PDBe 4dl1

X-ray diffraction
2Å resolution

Crystal Structure of human Myeloperoxidase with covalent thioxanthine analog

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Myeloperoxidase light chain Chains: A, B, E, F, I, J, M, N
Molecule details ›
Chains: A, B, E, F, I, J, M, N
Length: 104 amino acids
Theoretical weight: 11.9 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 167-270; Coverage: 15%)
Gene name: MPO
Myeloperoxidase heavy chain Chains: C, D, G, H, K, L, O, P
Molecule details ›
Chains: C, D, G, H, K, L, O, P
Length: 466 amino acids
Theoretical weight: 53.23 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 279-744; Coverage: 67%)
Gene name: MPO
Structure domains: Haem peroxidase domain superfamily, animal type

Ligands and Environments


Cofactor: Ligand HEM 8 x HEM

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 63.829Å b: 242.636Å c: 151.505Å
α: 90° β: 91.19° γ: 90°
R-values:
R R work R free
0.193 0.19 0.246