› 1bgp

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF BARLEY GRAIN PEROXIDASE 1

Released:
DOI: 10.2210/pdb1bgp/pdb
PDB entry 1bgp coloured by chain, front view.
PDB entry 1bgp coloured by chain, side view.
PDB entry 1bgp coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH.
Henriksen A, Welinder KG, Gajhede M
J Biol Chem 273 2241-8 (1998)
PMID: 9442067

Function and Biology Details

Reaction catalysed: 
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174920 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxidase Chain: A
Molecule details ›
Chain: A
Length: 309 amino acids
Theoretical weight: 33.87 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: Q40069 (Residues: 29-337; Coverage: 93%)
Gene name: Prx5
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
2 bound ligands:
Ligand CA 1 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 71.92Å b: 105.06Å c: 40.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.23

Quick links

Citations

4 review citations

Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes.
Valderrama et al. (2002)
3 more

7 mentions without citation

Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases.
Zámocký et al. (2014)
6 more