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Crystal structure of substrate-free P450CAM at low [K+]

Analyse Crystal structure of substrate-free P450CAM at low [K+] in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3L62
Type: protein
Length: 400 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
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Camphor 5-monooxygenase (EC 1.14.15.1)	protein	400	50% helix, 12% strand	P00183

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A

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

Pockets

2 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	673	0.83	0.87	67	HEM
2	56	0.31	0.76	15	empty

Compared structures

3L62 · Crystal structure of substrate-free P450cam at low [K+] · 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 3L62 · PDBe 3L62 · UniProt P00183

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