The value crystal structure of apo quinone reductase 2 at 1.35A
Serriere, J., Boutin, J.A., Isabet, T., Antoine, M., Ferry, G.To be published.
Experimental Data Snapshot
Starting Model: experimental
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wwPDB Validation   3D Report Full Report
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Ribosyldihydronicotinamide dehydrogenase [quinone] | 231 | Homo sapiens | Mutation(s): 1  Gene Names: NQO2, NMOR2 EC: 1.10.99.2 (PDB Primary Data), 1.10.5.1 (UniProt) | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P16083 (Homo sapiens) Explore P16083  Go to UniProtKB:  P16083 | |||||
PHAROS:  P16083 GTEx:  ENSG00000124588  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P16083 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 2 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
GOL Query on GOL | C [auth A] D [auth A] E [auth A] F [auth A] H [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N | |||
ZN Query on ZN | G [auth A], J [auth B] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |
Length ( ? ) | Angle ( ? ) |
---|---|
a = 56.12 | ¦Á = 90 |
b = 83.2 | ¦Â = 90 |
c = 106.54 | ¦Ă = 90 |
Software Name | Purpose |
---|---|
XDS | data scaling |
MOLREP | phasing |
REFMAC | refinement |
XDS | data reduction |