1Q23

Crystal structure of Chloramphenicol acetyltransferase I complexed with Fusidic acid at 2.18 A resolution

PDB DOI: https://doi.org/10.2210/pdb1Q23/pdb

Classification: TRANSFERASE
Organism(s): Escherichia coli
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2003-07-23 Released: 2004-08-03
Deposition Author(s): Roidis, A., Kokkinidis, M.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.18 ?
R-Value Free: 0.263
R-Value Work: 0.192
R-Value Observed: 0.195

Starting Model: experimental
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Ligand Structure Quality Assessment

This is version 1.3 of the entry. See complete history.

Literature

Crystal structure of Chloramphenicol acetyltransferase I in the apoenzyme form and complexed with fusidic acid at 2.18 A resolution

Roidis, A., Kokkinidis, M.

To be published.

Macromolecule Content

Total Structure Weight: 314.55 kDa
Atom Count: 22,280
Modelled Residue Count: 2,563
Deposited Residue Count: 2,628
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Chloramphenicol acetyltransferase	A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	219	Escherichia coli	Mutation(s): 0 Gene Names: CAT OR HCM1.206 EC: 2.3.1.28
UniProt
Find proteins for P62577 (Escherichia coli) Explore P62577 Go to UniProtKB: P62577
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P62577
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FUA Query on FUA Download Ideal Coordinates CCD File SDF format, chain N [auth A] SDF format, chain O [auth B] SDF format, chain P [auth C] SDF format, chain Q [auth D] SDF format, chain R [auth E] SDF format, chain S [auth F] SDF format, chain T [auth G] SDF format, chain U [auth H] SDF format, chain V [auth I] SDF format, chain W [auth J] SDF format, chain X [auth K] SDF format, chain Y [auth L] MOL2 format, chain N [auth A] MOL2 format, chain O [auth B] MOL2 format, chain P [auth C] MOL2 format, chain Q [auth D] MOL2 format, chain R [auth E] MOL2 format, chain S [auth F] MOL2 format, chain T [auth G] MOL2 format, chain U [auth H] MOL2 format, chain V [auth I] MOL2 format, chain W [auth J] MOL2 format, chain X [auth K] MOL2 format, chain Y [auth L] mmCIF format, chain N [auth A] mmCIF format, chain O [auth B] mmCIF format, chain P [auth C] mmCIF format, chain Q [auth D] mmCIF format, chain R [auth E] mmCIF format, chain S [auth F] mmCIF format, chain T [auth G] mmCIF format, chain U [auth H] mmCIF format, chain V [auth I] mmCIF format, chain W [auth J] mmCIF format, chain X [auth K] mmCIF format, chain Y [auth L]	N [auth A] O [auth B] P [auth C] Q [auth D] R [auth E] N [auth A], O [auth B], P [auth C], Q [auth D], R [auth E], S [auth F], T [auth G], U [auth H], V [auth I], W [auth J], X [auth K], Y [auth L]	FUSIDIC ACID C₃₁ H₄₈ O₆ IECPWNUMDGFDKC-MZJAQBGESA-N		Interactions Focus chain N [auth A] Focus chain O [auth B] Focus chain P [auth C] Focus chain Q [auth D] Focus chain R [auth E] Focus chain S [auth F] Focus chain T [auth G] Focus chain U [auth H] Focus chain V [auth I] Focus chain W [auth J] Focus chain X [auth K] Focus chain Y [auth L] Interactions & Density Focus chain N [auth A] Focus chain O [auth B] Focus chain P [auth C] Focus chain Q [auth D] Focus chain R [auth E] Focus chain S [auth F] Focus chain T [auth G] Focus chain U [auth H] Focus chain V [auth I] Focus chain W [auth J] Focus chain X [auth K] Focus chain Y [auth L]
CA Query on CA Download Ideal Coordinates CCD File SDF format, chain M [auth A] MOL2 format, chain M [auth A] mmCIF format, chain M [auth A]	M [auth A]	CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N		Interactions Focus chain M [auth A] Interactions & Density Focus chain M [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.18 ?
R-Value Free: 0.263
R-Value Work: 0.192
R-Value Observed: 0.195
Space Group: P 1 2₁ 1

Unit Cell:

Length ( ? )	Angle ( ? )
a = 115.354	α = 90
b = 129.198	β = 108.3
c = 118.073	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
MOSFLM	data reduction
CCP4	data scaling
AMoRE	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2004-08-03

Deposition Author(s):

Roidis, A.

Kokkinidis, M.

Revision History (Full details and data files)

Version 1.0: 2004-08-03
Type: Initial release
Version 1.1: 2008-04-29
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2023-08-16
Changes: Data collection, Database references, Derived calculations, Refinement description

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Help and Resources

1Q23

Crystal structure of Chloramphenicol acetyltransferase I complexed with Fusidic acid at 2.18 A resolution

Crystal structure of Chloramphenicol acetyltransferase I in the apoenzyme form and complexed with fusidic acid at 2.18 A resolution

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)