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The crystal structure of azor (azoreductase) from escherichia COLI: azor in complex with dicoumarol

Analyse The crystal structure of azor (azoreductase) from escherichia COLI: azor in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Z9C
Type
protein
Length
197 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
FMN-dependent NADH-azoreductase
EC
1.7.1.6
UniProt
P41407
Ligands
FMN, DTC
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFMN-dependent NADH-azoreductase (EC 1.7.1.6)protein19744% helix, 21% strandP41407

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · chains A
  • DTC · Bishydroxy[2h-1-benzopyran-2-one,1,2-benzopyrone] · ligand · chains A
  • GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.330.7713FMN

Compared structures

  • 2Z9C · The crystal structure of AzoR (azoreductase) from Escherichia coli: AzoR in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P41407 · AlphaFold monomer V2.0 prediction for FMN-dependent NADH:QUINONE oxidoreductase (P41407) · a predicted model of the same protein · chain A against A, TM-score 0.99

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