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Crystal structure of P450CAM

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

PDB
3WRJ
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 · 52% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, ECamphor 5-monooxygenase (EC 1.14.15.1)protein40552% helix, 11% strandP00183

Ligands and binding sites

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

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14380.870.9450HEM, CAM
24530.860.9352HEM, CAM
37640.690.7676empty
4680.300.7417empty
5520.280.7516empty

Interfaces

1 interface between chains.

  • A–E · 331 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 3WRJ · Crystal structure of P450cam · 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

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