› 4j6c

X-ray diffraction
1.9Å resolution

The 1.9 A crystal structure of CYP154C5 from Nocardia farcinica in complex with progesterone

Released:
DOI: 10.2210/pdb4j6c/pdb
PDB entry 4j6c coloured by chain, front view.
PDB entry 4j6c coloured by chain, side view.
PDB entry 4j6c coloured by chain, top view.
Source organism: Nocardia farcinica IFM 10152
Primary publication:
Enzyme-substrate complex structures of CYP154C5 shed light on its mode of highly selective steroid hydroxylation.
Herzog K, Bracco P, Onoda A, Hayashi T, Hoffmann K, Schallmey A
Acta Crystallogr D Biol Crystallogr 70 2875-89 (2014)
PMID: 25372679

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-178537 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 monooxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 410 amino acids
Theoretical weight: 45.38 KDa
Source organism: Nocardia farcinica IFM 10152
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5YNS8 (Residues: 1-410; Coverage: 100%)
Gene name: NFA_53110
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

5 bound ligands:
Ligand STR 2 x STR
Ligand HEM 2 x HEM
Ligand MG 2 x MG
Ligand FMT 4 x FMT
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: R3
Unit cell:
a: 102.999Å b: 102.999Å c: 217.86Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.192 0.238
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.
Szaleniec et al. (2018)
9 other articles

2 mentions without citation

Recent Structural Insights into Cytochrome P450 Function.
Guengerich et al. (2016)
1 more