› 4egm

X-ray diffraction
2.91Å resolution

The X-ray crystal structure of CYP199A4 in complex with 4-ethylbenzoic acid

Released:
DOI: 10.2210/pdb4egm/pdb
PDB entry 4egm coloured by chain, front view.
PDB entry 4egm coloured by chain, side view.
PDB entry 4egm coloured by chain, top view.
Source organism: Rhodopseudomonas palustris HaA2
Primary publication:
Investigation of the substrate range of CYP199A4: modification of the partition between hydroxylation and desaturation activities by substrate and protein engineering.
Bell SG, Zhou R, Yang W, Tan AB, Gentleman AS, Wong LL, Zhou W
Chemistry 18 16677-88 (2012)
PMID: 23135838

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 410 amino acids
Theoretical weight: 44.59 KDa
Source organism: Rhodopseudomonas palustris HaA2
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2IU02 (Residues: 1-410; Coverage: 100%)
Gene name: RPB_3613
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

5 bound ligands:
Ligand HEM 4 x HEM
Ligand EGM 4 x EGM
Ligand CL 4 x CL
Ligand GOL 4 x GOL
Ligand SO4 15 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 106.864Å b: 143.279Å c: 172.513Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.249
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Expanding P450 catalytic reaction space through evolution and engineering.
McIntosh et al. (2014)
1 more

1 mention without citation

Exploring the Factors which Result in Cytochrome P450 Catalyzed Desaturation Versus Hydroxylation.
Coleman et al. (2022)