› 1brt

X-ray diffraction
1.5Å resolution

BROMOPEROXIDASE A2 MUTANT M99T

Released:
DOI: 10.2210/pdb1brt/pdb
PDB entry 1brt coloured by chain, front view.
PDB entry 1brt coloured by chain, side view.
PDB entry 1brt 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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151563 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Non-haem bromoperoxidase BPO-A2 Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 30.25 KDa
Source organism: Kitasatospora aureofaciens
Expression system: Streptomyces lividans
UniProt:
  • Canonical: P29715 (Residues: 2-278; Coverage: 100%)
Gene name: bpoA2
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: I23
Unit cell:
a: 121.72Å b: 121.72Å c: 121.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.147 0.164
Expression system: Streptomyces lividans

Quick links

Citations

18 review citations

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

13 mentions without citation

Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction.
Xiang et al. (2002)
12 more