› 1pjp

X-ray diffraction
2.2Å resolution

THE 2.2 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE

Released:
DOI: 10.2210/pdb1pjp/pdb
PDB entry 1pjp coloured by chain, front view.
PDB entry 1pjp coloured by chain, side view.
PDB entry 1pjp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity.
Pereira PJ, Wang ZM, Rubin H, Huber R, Bode W, Schechter NM, Strobl S
J Mol Biol 286 163-73 (1999)
PMID: 9931257

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Phe-|- > Tyr-|- > Trp-|- > Leu-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150126 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymase Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 24.99 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P23946 (Residues: 22-247; Coverage: 99%)
Gene names: CMA1, CYH, CYM
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE INHIBITOR Chain: I
Molecule details ›
Chain: I
Length: 6 amino acids
Theoretical weight: 539 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand NAG 2 x NAG
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43
Unit cell:
a: 74.37Å b: 74.37Å c: 50.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.237
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

3 review citations

Intracellular proteoglycans.
Kolset et al. (2004)
2 more

4 mentions without citation

Mast cell peptidases: chameleons of innate immunity and host defense.
Trivedi et al. (2010)
3 more