7lag

X-ray diffraction
2.85Å resolution

CRYSTAL STRUCTURE OF MYELOPEROXIDASE SUBFORM C (MPO) COMPLEX WITH Compound-14 AKA 7-({1-[(3-phenoxyphenyl)methyl]-1H-pyrazol-4-yl}methyl)-3H-[1,2,3]triazolo[4,5-b]pyridin-5-amine

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-138570 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (4 distinct):
Myeloperoxidase light chain Chains: A, D, F, H
Molecule details ›
Chains: A, D, F, H
Length: 105 amino acids
Theoretical weight: 11.97 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 167-271; Coverage: 15%)
Gene name: MPO
Myeloperoxidase heavy chain Chains: B, E, G, I
Molecule details ›
Chains: B, E, G, I
Length: 466 amino acids
Theoretical weight: 53.22 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P05164 (Residues: 279-744; Coverage: 67%)
Gene name: MPO
Sequence domains: Animal haem peroxidase

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2221
Unit cell:
a: 143.459Å b: 149.886Å c: 228.642Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.235