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Crystal structure of a putative nitroreductase in complex with FMN (EXIG_2970) from exiguobacterium sibiricum 255-15 at 1.85 a resolution

Analyse Crystal structure of a putative nitroreductase in complex with FMN (EXIG_2970)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GE6
Type: protein
Length: 420 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitroreductase
UniProt: B1YG32
Ligands: FMN
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nitroreductase	protein	210	48% helix, 17% strand	B1YG32

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	638	0.72	0.79	55	FMN
2	667	0.71	0.78	53	FMN

Interfaces

1 interface between chains.

A–B · 3116 Å² buried · 46 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

3GE6 · Crystal structure of a putative nitroreductase in complex with FMN (EXIG_2970) from… · 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 B1YG32
Elsewhere: RCSB PDB 3GE6 · PDBe 3GE6 · UniProt B1YG32

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