› 4c9m

X-ray diffraction
1.8Å resolution

Structure of substrate free, glycerol bound wild type CYP101D1

Released:
DOI: 10.2210/pdb4c9m/pdb
PDB entry 4c9m coloured by chain, front view.
PDB entry 4c9m coloured by chain, side view.
PDB entry 4c9m coloured by chain, top view.
Source organism: Novosphingobium aromaticivorans
Primary publication:
Crystal structures and functional characterization of wild-type CYP101D1 and its active site mutants.
Batabyal D, Poulos TL
Biochemistry 52 8898-906 (2013)
PMID: 24261604

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 Chains: A, B
Molecule details ›
Chains: A, B
Length: 421 amino acids
Theoretical weight: 47.34 KDa
Source organism: Novosphingobium aromaticivorans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2GB12 (Residues: 1-421; Coverage: 100%)
Gene name: Saro_0514
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

2 bound ligands:
Ligand HEM 2 x HEM
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P6422
Unit cell:
a: 151.52Å b: 151.52Å c: 195.682Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 0.154 0.188
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Updating the Paradigm: Redox Partner Binding and Conformational Dynamics in Cytochromes P450.
Poulos et al. (2022)
12 other articles

1 mention without citation

Crystal structures and functional characterization of wild-type CYP101D1 and its active site mutants.
Batabyal et al. (2013)