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Crystal structure of cytochrome P450REVI

Analyse Crystal structure of cytochrome P450REVI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WVS
Type: protein
Length: 393 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative monooxygenase
UniProt: G1UDU7
Ligands: HEM, RRM
Pockets: 3 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative monooxygenase	protein	393	52% helix, 11% strand	G1UDU7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
RRM · (2E,4S,5S,6E,8E)-10-{(2R,3S,6S,8R,9S)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl}-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid · ligand · chains A
GOL · Glycerol · additive · 5 copies · chains A
TLA · L(+)-tartaric acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1160	0.86	0.87	101	HEM, RRM, GOL
2	101	0.46	0.80	20	empty
3	146	0.44	0.75	21	empty

Compared structures

3WVS · Crystal Structure of Cytochrome P450revI · 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 G1UDU7
Elsewhere: RCSB PDB 3WVS · PDBe 3WVS · UniProt G1UDU7

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