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Camphor bound P450CAM D251E structure

Analyse Camphor bound P450CAM D251E structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WE6
Type: protein
Length: 810 residues
Chains: 2
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, CAM, K
Pockets: 6 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Camphor 5-monooxygenase (EC 1.14.15.1)	protein	405	50% helix, 11% strand	P00183

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
CAM · Camphor · ligand · 2 copies · chains A, B
K · Potassium ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	494	0.87	0.93	52	HEM, CAM
2	493	0.87	0.93	57	HEM, CAM
3	906	0.72	0.76	73	empty
4	58	0.38	0.80	15	empty
5	76	0.37	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 233 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6WE6 · Camphor bound P450cam D251E structure · 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 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 P00183
Elsewhere: RCSB PDB 6WE6 · PDBe 6WE6 · UniProt P00183

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