MolNFT v1 · #138467 · protein

P450CAM mutant R186A

5WK7 · Camphor 5-monooxygenase: “P450CAM mutant R186A”. X-ray diffraction, 3 ligands (HEM, CAH, K), 4 pockets (best druggability 0.85). MolNFT v1 #138467 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5WK7
Type: protein
Length: 405 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Camphor 5-monooxygenase
EC: 1.14.15.1
UniProt: P00183
Ligands: HEM, CAH, K
Pockets: 4 · best druggability 0.85

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camphor 5-monooxygenase (EC 1.14.15.1)	protein	405	52% helix, 11% strand	P00183

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CAH · 5-exo-hydroxycamphor · ligand · chains A
K · Potassium ion · metal · chains A

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

Pockets

4 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	410	0.85	0.93	48	HEM, CAH
2	63	0.35	0.78	17	empty
3	59	0.30	0.75	17	empty
4	54	0.30	0.76	17	empty

Compared structures

5WK7 · P450cam mutant R186A · the same entry in another collection · chain A against A, TM-score 1.00
P00183 · AlphaFold monomer V2.0 prediction for camphor 5-monooxygenase (P00183) · 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 P00183
Elsewhere: RCSB PDB 5WK7 · PDBe 5WK7 · UniProt P00183

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