› 5b72

X-ray diffraction
1.98Å resolution

Crystal structure of bovine lactoperoxidase with a broken covalent bond between Glu258 and heme moiety at 1.98 A resolution.

Released:
DOI: 10.2210/pdb5b72/pdb
PDB entry 5b72 coloured by chain, front view.
PDB entry 5b72 coloured by chain, side view.
PDB entry 5b72 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98Å resolution.
Singh PK, Sirohi HV, Iqbal N, Tiwari P, Kaur P, Sharma S, Singh TP
Biochim Biophys Acta Proteins Proteom 1865 329-335 (2017)
PMID: 27986533

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160329 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lactoperoxidase Chain: A
Molecule details ›
Chain: A
Length: 595 amino acids
Theoretical weight: 67.74 KDa
Source organism: Bos taurus
Expression system: Bos taurus
UniProt:
  • Canonical: P80025 (Residues: 118-712; Coverage: 86%)
Gene name: LPO
Sequence domains: Animal haem peroxidase
Structure domains: Haem peroxidase domain superfamily, animal type

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
6 bound ligands:
Ligand SO4 1 x SO4
Ligand OSM 1 x OSM
Ligand IOD 9 x IOD
Ligand PGE 2 x PGE
Ligand NAG 3 x NAG
Ligand CA 1 x CA
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 53.847Å b: 80.192Å c: 75.086Å
α: 90° β: 105.41° γ: 90°
R-values:
R R work R free
0.19 0.188 0.235
Expression system: Bos taurus

Quick links

Citations

3 citation in other articles

Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated Human Peroxidasin 1.
Paumann-Page et al. (2017)
2 more

1 mention without citation

Structures of mouse DUOX1-DUOXA1 provide mechanistic insights into enzyme activation and regulation.
Sun J. (2020)