› 6dwm

X-ray diffraction
2.85Å resolution

Structure of Human Cytochrome P450 1A1 with Bergamottin

Released:
DOI: 10.2210/pdb6dwm/pdb
PDB entry 6dwm coloured by chain, front view.
PDB entry 6dwm coloured by chain, side view.
PDB entry 6dwm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human cytochrome P450 1A1 with bergamottin and erlotinib reveal active-site modifications for binding of diverse ligands.
Bart AG, Scott EE
J Biol Chem 293 19201-19210 (2018)
PMID: 30254074

Function and Biology Details

Reactions catalysed: 
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
A hydroperoxy icosatetraenoate = an oxoicosatetraenoate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 1A1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 491 amino acids
Theoretical weight: 55.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04798 (Residues: 35-512; Coverage: 93%)
Gene name: CYP1A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
3 bound ligands:
Ligand HJJ 4 x HJJ
Ligand CPS 2 x CPS
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 65.33Å b: 194.758Å c: 236.137Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.24
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Globally Approved EGFR Inhibitors: Insights into Their Syntheses, Target Kinases, Biological Activities, Receptor Interactions, and Metabolism.
Abourehab et al. (2021)
3 more

5 mentions without citation

Structures of human cytochrome P450 1A1 with bergamottin and erlotinib reveal active-site modifications for binding of diverse ligands.
Bart et al. (2018)
4 more