MolNFT v1 · #123677 · protein

The crystal structure of azoreductase from yersinia pestis CO92 in its apo form

5JRO · FMN-dependent NADH-azoreductase: “The crystal structure of azoreductase from yersinia pestis CO92 in its apo form”. X-ray diffraction, 3 pockets (best druggability 0.54). MolNFT v1 #123677 on GenesisL1: 3D structure, binding sites…

PDB: 5JRO
Type: protein
Length: 366 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FMN-dependent NADH-azoreductase
EC: 1.7.-.-
UniProt: Q8ZE60
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FMN-dependent NADH-azoreductase (EC 1.7.-.-)	protein	184	40% helix, 21% strand	Q8ZE60
B	FMN-dependent NADH-azoreductase (EC 1.7.-.-)	protein	182	42% helix, 23% strand	Q8ZE60

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	233	0.54	0.76	19	GOL
2	69	0.42	0.81	20	empty
3	114	0.41	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 1213 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

Q8ZE60 · AlphaFold monomer V2.0 prediction for FMN-dependent NADH:QUINONE oxidoreductase (Q8ZE60) · a predicted model of the same protein · chain B against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8ZE60
Elsewhere: RCSB PDB 5JRO · PDBe 5JRO · UniProt Q8ZE60

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