MolNFT v1 · #122267 · protein

Open state of P450CAM after soaking in camphor

5IK1 · Camphor 5-monooxygenase: “Open state of P450CAM after soaking in camphor”. X-ray diffraction, 2 ligands (CAM, HEM), 3 pockets (best druggability 0.81). MolNFT v1 #122267 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5IK1
Type: protein
Length: 394 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: CAM, HEM
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camphor 5-monooxygenase (EC 1.14.15.1)	protein	394	51% helix, 11% strand	P00183

Ligands and binding sites

CAM · Camphor · ligand · 2 copies · chains A
HEM · Protoporphyrin IX containing Fe · ligand · 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	1004	0.81	0.82	73	HEM, CAM
2	72	0.45	0.82	23	empty
3	65	0.35	0.77	15	empty

Compared structures

5IK1 · Open state of P450cam after soaking in camphor · 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 0.95

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 5IK1 · PDBe 5IK1 · UniProt P00183

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