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Crystal structure of the P450CAM G248T mutant in the cyanide bound state

Analyse Crystal structure of the P450CAM G248T mutant in the cyanide bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QBM
Type
protein
Length
405 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome P450-cam
EC
1.14.15.1
UniProt
P00183
Ligands
HEM, CAM, K, CYN
Pockets
2 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACytochrome P450-cam (EC 1.14.15.1)protein40553% helix, 10% strandP00183

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • CAM · Camphor · ligand · chains A
  • K · Potassium ion · metal · chains A
  • CYN · Cyanide ion · ion · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14180.870.9450CYN, HEM, CAM
2630.310.7519empty

Compared structures

  • 2QBM · Crystal structure of the P450cam G248T mutant in the cyanide bound state · 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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