› 6gmf

X-ray diffraction
1.55Å resolution

Structure of Cytochrome P450 CYP109Q5 from Chondromyces apiculatus

Released:
DOI: 10.2210/pdb6gmf/pdb
PDB 6gmf coloured by chain and viewed from the front.
PDB 6gmf coloured by chain and viewed from the side.
PDB 6gmf coloured by chain and viewed from the top.
Source organism: Chondromyces apiculatus DSM 436
Primary publication:
Characterization and structure-guided engineering of the novel versatile terpene monooxygenase CYP109Q5 from Chondromyces apiculatus DSM436.
Klenk JM, Dubiel P, Sharma M, Grogan G, Hauer B
Microb Biotechnol 12 377-391 (2019)
PMID: 30592153

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 Chain: A
Molecule details ›
Chain: A
Length: 397 amino acids
Theoretical weight: 43.92 KDa
Source organism: Chondromyces apiculatus DSM 436
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A017T5A5 (Residues: 1-397; Coverage: 100%)
Gene name: CAP_4855
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

1 bound ligand:
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 44.69Å b: 55.02Å c: 74.8Å
α: 90° β: 91.67° γ: 90°
R-values:
R R work R free
0.187 0.185 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Identification of a self-sufficient cytochrome P450 monooxygenase from Cupriavidus pinatubonensis JMP134 involved in 2-hydroxyphenylacetic acid catabolism, via homogentisate pathway.
Donoso et al. (2021)
1 more

1 mention without citation

Characterization and structure-guided engineering of the novel versatile terpene monooxygenase CYP109Q5 from Chondromyces apiculatus DSM436.
Klenk et al. (2019)