› 7oih

X-ray diffraction
2.6Å resolution

Glycosylation in the crystal structure of neutrophil myeloperoxidase

Released:
DOI: 10.2210/pdb7oih/pdb
PDB entry 7oih coloured by chain, front view.
PDB entry 7oih coloured by chain, side view.
PDB entry 7oih coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Native glycosylation and binding of the antidepressant paroxetine in a low-resolution crystal structure of human myeloperoxidase.
Krawczyk L, Semwal S, Soubhye J, Lemri Ouadriri S, Prévost M, Van Antwerpen P, Roos G, Bouckaert J
Acta Crystallogr D Struct Biol 78 1099-1109 (2022)
PMID: 36048150

Function and Biology Details

Reaction catalysed: 
Cl(-) + H(2)O(2) + H(+) = HClO + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138573 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (9 distinct):
Myeloperoxidase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 579 amino acids
Theoretical weight: 66.01 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 166-744; Coverage: 83%)
Gene name: MPO
Sequence domains: Animal haem peroxidase

Ligands and Environments


Cofactor: Ligand HEM 8 x HEM
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
6 bound ligands:
Ligand CL 36 x CL
Ligand CA 8 x CA
Ligand SCN 10 x SCN
Ligand 8PR 4 x 8PR
Ligand PO4 14 x PO4
Ligand NAG 5 x NAG
1 modified residue:
Ligand CSO 8 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2
Unit cell:
a: 155.91Å b: 144.634Å c: 236.454Å
α: 90° β: 91.526° γ: 90°
R-values:
R R work R free
0.179 0.179 0.22

Quick links

Citations

1 citations in other articles

Posttranslational modification and heme cavity architecture of human eosinophil peroxidase-insights from first crystal structure and biochemical characterization.
Pfanzagl et al. (2023)

1 mention without citation

Native glycosylation and binding of the antidepressant paroxetine in a low-resolution crystal structure of human myeloperoxidase.
Krawczyk et al. (2022)