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FMN-dependent nitroreductase (CDR20291_0767) from clostridium difficile R20291

Analyse FMN-dependent nitroreductase (CDR20291_0767) from clostridium difficile R20291 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J6C
Type: protein
Length: 346 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative reductase
UniProt: C9YJL7
Ligands: FMN
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative reductase	protein	173	38% helix, 22% strand	C9YJL7

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
IMD · Imidazole · additive · 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	189	0.55	0.80	27	IMD, FMN
2	186	0.55	0.80	28	FMN, IMD

Interfaces

1 interface between chains.

A–B · 3026 Å² buried · 56 hydrogen bonds · protein-protein

Compared structures

5J6C · FMN-dependent Nitroreductase (CDR20291_0767) from Clostridium difficile R20291 · 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 C9YJL7
Elsewhere: RCSB PDB 5J6C · PDBe 5J6C · UniProt C9YJL7

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