MolNFT v1 · #161947 · protein

Structure of azoreductase from bacillus sp. A01

6QU0 · FMN-dependent NADH-azoreductase: “Structure of azoreductase from bacillus sp. A01”. X-ray diffraction, 2 ligands (FMN, SO4), 4 pockets (best druggability 0.72). MolNFT v1 #161947 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6QU0
Type: protein
Length: 422 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FMN-dependent NADH-azoreductase
EC: 1.7.-.-
UniProt: A0A0B0IKH9
Ligands: FMN, SO4
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	FMN-dependent NADH-azoreductase (EC 1.7.-.-)	protein	211	39% helix, 24% strand	A0A0B0IKH9

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · chains B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	390	0.72	0.83	33	FMN
2	383	0.71	0.82	42	FMN
3	249	0.60	0.80	28	GOL
4	51	0.26	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 1440 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6QU0 · Structure of azoreductase from Bacillus sp. A01 · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A0B0IKH9
Elsewhere: RCSB PDB 6QU0 · PDBe 6QU0 · UniProt A0A0B0IKH9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.