› 5wv3

X-ray diffraction
2.07Å resolution

Crystal structure of bovine lactoperoxidase with a partial Glu258-heme linkage at 2.07 A resolution.

Released:
DOI: 10.2210/pdb5wv3/pdb
PDB entry 5wv3 coloured by chain, front view.
PDB entry 5wv3 coloured by chain, side view.
PDB entry 5wv3 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural basis of activation of mammalian heme peroxidases.
Singh PK, Iqbal N, Sirohi HV, Bairagya HR, Kaur P, Sharma S, Singh TP
Prog Biophys Mol Biol 133 49-55 (2018)
PMID: 29174286

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: 67.84 KDa
Source organism: 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 CA 1 x CA
Ligand NAG 3 x NAG
Ligand IOD 3 x IOD
Ligand OSM 10 x OSM
Ligand GOL 2 x GOL
Ligand BR 1 x BR
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: 54.012Å b: 79.809Å c: 66.106Å
α: 90° β: 93.01° γ: 90°
R-values:
R R work R free
0.169 0.167 0.236

Quick links

Citations

3 review citations

ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications.
Moldogazieva et al. (2018)
2 more