› 3cv9

X-ray diffraction
1.7Å resolution

Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (R73A/R84A mutant) in complex with 1alpha,25-dihydroxyvitamin D3

Released:
DOI: 10.2210/pdb3cv9/pdb
PDB entry 3cv9 coloured by chain, front view.
PDB entry 3cv9 coloured by chain, side view.
PDB entry 3cv9 coloured by chain, top view.
Source organism: Streptomyces griseolus
Primary publication:
Structure-based design of a highly active vitamin D hydroxylase from Streptomyces griseolus CYP105A1.
Hayashi K, Sugimoto H, Shinkyo R, Yamada M, Ikeda S, Ikushiro S, Kamakura M, Shiro Y, Sakaki T
Biochemistry 47 11964-72 (2008)
PMID: 18937506

Function and Biology Details

Reaction catalysed: 
Calcidiol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = calcitriol + 2 oxidized ferredoxin [iron-sulfur] cluster + 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-148353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vitamin D3 dihydroxylase Chain: A
Molecule details ›
Chain: A
Length: 412 amino acids
Theoretical weight: 44.91 KDa
Source organism: Streptomyces griseolus
Expression system: Escherichia coli
UniProt:
  • Canonical: P18326 (Residues: 1-406; Coverage: 100%)
Gene names: cyp105A1, suaC
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

2 bound ligands:
Ligand HEM 1 x HEM
Ligand VDX 1 x VDX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P212121
Unit cell:
a: 53.315Å b: 53.659Å c: 140.605Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.199 0.253
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Cytochromes P450 as promising catalysts for biotechnological application: chances and limitations.
Bernhardt et al. (2014)
6 more

2 mentions without citation

Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.
Rudolf et al. (2017)
1 more