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Crystal structure of N-(1-PYRENE)ACETAMIDE labeled P450CAM in substrate bound form.

Analyse Crystal structure of N-(1-PYRENE)ACETAMIDE labeled P450CAM in substrate bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4KKY
Type
protein
Length
411 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, 1T4, CAM, K
Pockets
1 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XCamphor 5-monooxygenase (EC 1.14.15.1)protein41151% helix, 10% strandP00183

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains X
  • 1T4 · N-(pyren-1-yl)acetamide · ligand · chains X
  • CAM · Camphor · ligand · chains X
  • K · Potassium ion · metal · 2 copies · chains X

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14310.870.9448HEM, CAM

Compared structures

  • 4KKY · Crystal structure of N-(1-Pyrene)acetamide labeled P450cam in substrate bound form. · the same entry in another collection · chain X against X, TM-score 1.00
  • P00183 · AlphaFold monomer V2.0 prediction for camphor 5-monooxygenase (P00183) · a predicted model of the same protein · chain X against A, TM-score 0.99

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