9F5X | pdb_00009f5x

Structure of the Chlamydomonas reinhardtii respiratory supercomplex I1 III2 IV2


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.82 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

In-cell architecture of the mitochondrial respiratory chain

Waltz, F.Righetto, R.Lamm, L.Salinas-Giege, T.Kelley, R.Zhang, X.Obr, M.Khavnekar, S.Kotecha, A.Engel, B.D.

(2025) Science 


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome bA [auth 1A],
B [auth 1B]
381Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome b-c1 complex subunit Rieske, mitochondrialC [auth 1C],
D [auth 1D]
262Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.8
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome c1E [auth 1E],
F [auth 1F]
314Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.10.2.2
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Complex III subunit 9G [auth 1G],
H [auth 1H]
60Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome b-c1 complex subunit 6I [auth 1I],
J [auth 1J]
69Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8K [auth 1K],
L [auth 1L]
73Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.10.2.2
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
MPP-BetaM [auth 1M],
N [auth 1N]
495Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10O [auth 1O],
P [auth 1P]
59Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.10.2.2
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha-MPPQ [auth 1Q],
S [auth 1S]
485Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome b-c1 complex subunit 7R [auth 1R],
T [auth 1T]
123Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome c oxidase subunit 1GA [auth 3A],
U [auth 2A]
504Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.9
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome c oxidase polypeptide IIHA [auth 3B],
V [auth 2B]
284Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
cytochrome-c oxidaseIA [auth 3C],
W [auth 2C]
153Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.9
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Entity ID: 14
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome c oxidase subunit 3JA [auth 3D],
X [auth 2D]
382Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 15
MoleculeChains Sequence LengthOrganismDetailsImage
Cox5bKA [auth 3E],
Y [auth 2E]
175Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 16
MoleculeChains Sequence LengthOrganismDetailsImage
Cox5cLA [auth 3F],
Z [auth 2F]
96Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 17
MoleculeChains Sequence LengthOrganismDetailsImage
Cox6aAA [auth 2G],
MA [auth 3G]
125Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 18
MoleculeChains Sequence LengthOrganismDetailsImage
Cox6bBA [auth 2H],
NA [auth 3H]
148Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 19
MoleculeChains Sequence LengthOrganismDetailsImage
Cox7cCA [auth 2I],
OA [auth 3I]
101Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 20
MoleculeChains Sequence LengthOrganismDetailsImage
Cytochrome c oxidase subunitDA [auth 2J],
PA [auth 3J]
105Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 21
MoleculeChains Sequence LengthOrganismDetailsImage
Cox7aEA [auth 2K],
QA [auth 3K]
58Chlamydomonas reinhardtiiMutation(s): 0 
UniProt
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Entity ID: 22
MoleculeChains Sequence LengthOrganismDetailsImage
CoxInFA [auth 2L],
RA [auth 3L]
87Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 23
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase 24 kD subunitSA [auth A]282Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3
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Entity ID: 24
MoleculeChains Sequence LengthOrganismDetailsImage
NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrialTA [auth B]484Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.2
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Entity ID: 25
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase 78 kDa subunitUA [auth C]733Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 26
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase 30kDa subunit domain-containing proteinVA [auth D]282Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 27
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase 49 kD subunitWA [auth E]467Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3
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Entity ID: 28
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase subunit 10XA [auth F]164Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3
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Entity ID: 29
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase subunit 8YA [auth G]231Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3
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Entity ID: 30
MoleculeChains Sequence LengthOrganismDetailsImage
B14.5aZA [auth H]118Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 31
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 18 kDa subunitAB [auth I]165Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3
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Entity ID: 32
MoleculeChains Sequence LengthOrganismDetailsImage
Acyl carrier proteinBB [auth J],
JC [auth r]
128Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 33
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase B14 subunitCB [auth K]138Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 34
MoleculeChains Sequence LengthOrganismDetailsImage
NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrialDB [auth L]187Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 35
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase 13 kD-like subunitEB [auth M]154Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 36
MoleculeChains Sequence LengthOrganismDetailsImage
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12FB [auth N]156Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 37
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase B8 subunitGB [auth O]101Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3
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Entity ID: 38
MoleculeChains Sequence LengthOrganismDetailsImage
Putative NADH:ubiquinone oxidoreductase 39 kDa subunitHB [auth P]397Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 39
MoleculeChains Sequence LengthOrganismDetailsImage
NADH-ubiquinone oxidoreductase chain 1IB [auth Q]292Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.2
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Entity ID: 40
MoleculeChains Sequence LengthOrganismDetailsImage
NADH-ubiquinone oxidoreductase chain 2JB [auth R]387Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.2
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Entity ID: 41
MoleculeChains Sequence LengthOrganismDetailsImage
NADH-ubiquinone oxidoreductase chain 3KB [auth S]279Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 42
MoleculeChains Sequence LengthOrganismDetailsImage
NADH-ubiquinone oxidoreductase chain 4LB [auth T]443Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.2
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Entity ID: 43
MoleculeChains Sequence LengthOrganismDetailsImage
NADH dehydrogenase subunit 4LMB [auth U]227Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 44
MoleculeChains Sequence LengthOrganismDetailsImage
NADH-ubiquinone oxidoreductase chain 5NB [auth V]546Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.2
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Entity ID: 45
MoleculeChains Sequence LengthOrganismDetailsImage
NADH-ubiquinone oxidoreductase chain 6OB [auth W]162Chlamydomonas reinhardtiiMutation(s): 0 
EC: 7.1.1.2
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Entity ID: 46
MoleculeChains Sequence LengthOrganismDetailsImage
ASHIPB [auth X]149Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 47
MoleculeChains Sequence LengthOrganismDetailsImage
P9QB [auth Y]64Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 48
MoleculeChains Sequence LengthOrganismDetailsImage
KFYIRB [auth Z]124Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 49
MoleculeChains Sequence LengthOrganismDetailsImage
AGGGSB [auth a]129Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 50
MoleculeChains Sequence LengthOrganismDetailsImage
ESSSTB [auth b]172Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 51
MoleculeChains Sequence LengthOrganismDetailsImage
B9UB [auth c]67Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 52
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 10 kDa subunitVB [auth d]86Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 53
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 23 kDa subunitWB [auth e]219Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 54
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 7.5 kDa subunitXB [auth f]65Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 55
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial putative NADH:ubiquinone oxidoreductase 6.5 kDa subunitYB [auth g]55Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 56
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 13 kDa subunitZB [auth h]142Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 57
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase 15 kDa subunit-likeAC [auth i]81Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 58
MoleculeChains Sequence LengthOrganismDetailsImage
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7BC [auth j]86Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 59
MoleculeChains Sequence LengthOrganismDetailsImage
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9CC [auth k]117Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 60
MoleculeChains Sequence LengthOrganismDetailsImage
NADH:ubiquinone oxidoreductase 20,9 kD-like subunitDC [auth l]121Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 61
MoleculeChains Sequence LengthOrganismDetailsImage
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13EC [auth m]142Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 62
MoleculeChains Sequence LengthOrganismDetailsImage
Putative NADH:ubiquinone oxidoreductase 12.5 kDa subunitFC [auth n]106Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 63
MoleculeChains Sequence LengthOrganismDetailsImage
Putative NADH:ubiquinone oxidoreductase 17.8 kDa subunitGC [auth o]155Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 64
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 16 kDa subunitHC [auth p]130Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 65
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 19 kDa subunitIC [auth q]197Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 66
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 32 kDa subunitKC [auth s]312Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 67
MoleculeChains Sequence LengthOrganismDetailsImage
CAG2 - CA-likeLC [auth t]279Chlamydomonas reinhardtiiMutation(s): 0 
UniProt
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Entity ID: 68
MoleculeChains Sequence LengthOrganismDetailsImage
CAG1MC [auth u]229Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 69
MoleculeChains Sequence LengthOrganismDetailsImage
P10NC [auth v]45Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 70
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial NADH:ubiquinone oxidoreductase 9 kDa subunitOC [auth w]109Chlamydomonas reinhardtiiMutation(s): 0 
EC: 1.6.5.3 (PDB Primary Data), 1.6.99.3 (PDB Primary Data)
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Entity ID: 71
MoleculeChains Sequence LengthOrganismDetailsImage
NUOP8PC [auth x]157Chlamydomonas reinhardtiiMutation(s): 0 
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Entity ID: 72
MoleculeChains Sequence LengthOrganismDetailsImage
NUOP7QC [auth y]118Chlamydomonas reinhardtiiMutation(s): 0 
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Small Molecules
Ligands 19 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CDL
Query on CDL

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BD [auth 1B]
ED [auth 1B]
FD [auth 1E]
HG [auth h]
JD [auth 1F]
BD [auth 1B],
ED [auth 1B],
FD [auth 1E],
HG [auth h],
JD [auth 1F],
JF [auth R],
NG [auth u],
OD [auth 1K],
OG [auth u],
QD [auth 1L],
QG [auth x],
RD [auth 1M],
TG [auth y],
VC [auth 1A],
VF [auth V],
ZF [auth W]
CARDIOLIPIN
C81 H156 O17 P2
XVTUQDWPJJBEHJ-KZCWQMDCSA-L
HEA
Query on HEA

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HE [auth 3A],
IE [auth 3A],
WD [auth 2A],
XD [auth 2A]
HEME-A
C49 H56 Fe N4 O6
ZGGYGTCPXNDTRV-PRYGPKJJSA-L
COO
Query on COO

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KG [auth s]CROTONYL COENZYME A
C25 H40 N7 O17 P3 S
KFWWCMJSYSSPSK-XBTRWLRFSA-N
PC7
Query on PC7

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AE [auth 2A]
EF [auth Q]
HF [auth R]
LE [auth 3A]
MD [auth 1G]
AE [auth 2A],
EF [auth Q],
HF [auth R],
LE [auth 3A],
MD [auth 1G],
MG [auth u],
ND [auth 1H],
PF [auth T]
(7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE
C42 H85 N O8 P
PZNPLUBHRSSFHT-FAIXQHPJSA-O
PGT
Query on PGT

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AG [auth b]
GE [auth 3A]
IG [auth l]
OF [auth T]
RF [auth T]
AG [auth b],
GE [auth 3A],
IG [auth l],
OF [auth T],
RF [auth T],
VD [auth 2A]
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE
C40 H79 O10 P
KBPVYRBBONZJHF-AMAPPZPBSA-N
NDP
Query on NDP

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CF [auth P]NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
C21 H30 N7 O17 P3
ACFIXJIJDZMPPO-NNYOXOHSSA-N
PTY
Query on PTY

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AF [auth G]
CE [auth 2D]
CG [auth e]
DG [auth e]
EE [auth 2F]
AF [auth G],
CE [auth 2D],
CG [auth e],
DG [auth e],
EE [auth 2F],
GF [auth R],
GG [auth h],
HD [auth 1E],
IF [auth R],
KF [auth R],
LD [auth 1F],
MF [auth S],
NE [auth 3D],
NF [auth T],
PE [auth 3F],
QF [auth T],
RG [auth x],
SF [auth T],
WF [auth V],
XF [auth V],
YF [auth V]
PHOSPHATIDYLETHANOLAMINE
C40 H80 N O8 P
NJGIRBISCGPRPF-KXQOOQHDSA-N
3PH
Query on 3PH

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BG [auth c]
CD [auth 1B]
DD [auth 1B]
DE [auth 2D]
EG [auth g]
BG [auth c],
CD [auth 1B],
DD [auth 1B],
DE [auth 2D],
EG [auth g],
FE [auth 2I],
FF [auth R],
FG [auth h],
GD [auth 1E],
LF [auth S],
OE [auth 3D],
PD [auth 1K],
PG [auth w],
QE [auth 3I],
SG [auth y],
TF [auth V],
UD [auth 1R],
UF [auth V],
WC [auth 1A]
1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE
C39 H77 O8 P
YFWHNAWEOZTIPI-DIPNUNPCSA-N
HEC
Query on HEC

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ID [auth 1E],
KD [auth 1F]
HEME C
C34 H34 Fe N4 O4
HXQIYSLZKNYNMH-LJNAALQVSA-N
HEM
Query on HEM

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AD [auth 1B],
TC [auth 1A],
UC [auth 1A],
ZC [auth 1B]
PROTOPORPHYRIN IX CONTAINING FE
C34 H32 Fe N4 O4
KABFMIBPWCXCRK-RGGAHWMASA-L
8Q1
Query on 8Q1

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BF [auth J],
JG [auth r]
S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
C23 H45 N2 O8 P S
MVHUOSAYFQKAMT-NRFANRHFSA-N
UQ5
Query on UQ5

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DF [auth Q],
RC [auth 1A],
SC [auth 1A],
XC [auth 1B],
YC [auth 1B]
2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE
C34 H50 O4
NYFAQDMDAFCWPU-UVCHAVPFSA-N
FMN
Query on FMN

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SE [auth B]FLAVIN MONONUCLEOTIDE
C17 H21 N4 O9 P
FVTCRASFADXXNN-SCRDCRAPSA-N
SF4
Query on SF4

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TE [auth B]
VE [auth C]
WE [auth C]
XE [auth F]
YE [auth G]
TE [auth B],
VE [auth C],
WE [auth C],
XE [auth F],
YE [auth G],
ZE [auth G]
IRON/SULFUR CLUSTER
Fe4 S4
LJBDFODJNLIPKO-UHFFFAOYSA-N
FES
Query on FES

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RE [auth A],
UE [auth C]
FE2/S2 (INORGANIC) CLUSTER
Fe2 S2
NIXDOXVAJZFRNF-UHFFFAOYSA-N
CUA
Query on CUA

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BE [auth 2C],
ME [auth 3C]
DINUCLEAR COPPER ION
Cu2
ALKZAGKDWUSJED-UHFFFAOYSA-N
ZN
Query on ZN

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LG [auth s],
SD [auth 1M],
TD [auth 1N]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
CU
Query on CU

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JE [auth 3A],
YD [auth 2A]
COPPER (II) ION
Cu
JPVYNHNXODAKFH-UHFFFAOYSA-N
MG
Query on MG

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KE [auth 3A],
ZD [auth 2A]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.82 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX1.20.1_4487:
RECONSTRUCTIONcryoSPARC

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Alexander von Humboldt FoundationGermany--
Swiss National Science FoundationSwitzerland210561

Revision History  (Full details and data files)

  • Version 1.0: 2025-03-12
    Type: Initial release
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