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Crystal structure of nitric reductase from denitrifying fungus fusarium oxysporum complex with carbon monoxide

Analyse Crystal structure of nitric reductase from denitrifying fungus fusarium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ROM
Type: protein
Length: 399 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450
UniProt: P23295
Ligands: HEM, CMO
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450	protein	399	52% helix, 10% strand	P23295

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CMO · Carbon monoxide · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1046	0.80	0.81	82	HEM, CMO

Compared structures

2ROM · Crystal structure of nitric reductase from denitrifying fungus fusarium oxysporum complex… · the same entry in another collection · chain A against A, TM-score 1.00
P23295 · AlphaFold monomer V2.0 prediction for NADP nitrous oxide-forming nitric oxide reductase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P23295
Elsewhere: RCSB PDB 2ROM · PDBe 2ROM · UniProt P23295

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