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Crystal structure of FMN and NADPH-dependent nitroreductase nfnb from sphigopyxis sp. strain hmh

Analyse Crystal structure of FMN and NADPH-dependent nitroreductase nfnb from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DP0
Type: protein
Length: 446 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitroreductase family protein
UniProt: A0A2L0VUJ4
Ligands: FMN
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nitroreductase family protein	protein	223	49% helix, 17% strand	A0A2L0VUJ4

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

4 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	433	0.74	0.84	41	FMN
2	494	0.72	0.82	44	FMN
3	95	0.38	0.76	17	empty
4	71	0.34	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 3679 Å² buried · 58 hydrogen bonds · protein-protein

Compared structures

7DP0 · Crystal structure of FMN and NADPH-dependent nitroreductase NfnB from sphigopyxis sp.… · 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 A0A2L0VUJ4
Elsewhere: RCSB PDB 7DP0 · PDBe 7DP0 · UniProt A0A2L0VUJ4

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