› 1a7u

X-ray diffraction
1.75Å resolution

CHLOROPEROXIDASE T

Released:
DOI: 10.2210/pdb1a7u/pdb
PDB entry 1a7u coloured by chain, front view.
PDB entry 1a7u coloured by chain, side view.
PDB entry 1a7u coloured by chain, top view.
Source organism: Kitasatospora aureofaciens
Primary publication:
Structural investigation of the cofactor-free chloroperoxidases.
Hofmann B, Tölzer S, Pelletier I, Altenbuchner J, van Pée KH, Hecht HJ
J Mol Biol 279 889-900 (1998)
PMID: 9642069

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Non-heme chloroperoxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 277 amino acids
Theoretical weight: 30.25 KDa
Source organism: Kitasatospora aureofaciens
Expression system: Streptomyces lividans
UniProt:
  • Canonical: O31168 (Residues: 2-278; Coverage: 100%)
Gene names: cpo, cpoT
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P213
Unit cell:
a: 126.56Å b: 126.56Å c: 126.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.152 0.176
Expression system: Streptomyces lividans

Quick links

Citations

17 review citations

Alpha/beta hydrolase fold enzymes: the family keeps growing.
Nardini et al. (1999)
16 more

7 mentions without citation

Characterizing the complexity of enzymes on the basis of their mechanisms and structures with a bio-computational analysis.
Holliday et al. (2011)
6 more