› 2rdl

X-ray diffraction
2.5Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130678 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase S1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 226 amino acids
Theoretical weight: 25.35 KDa
Source organism: Mesocricetus auratus
Expression system: unidentified baculovirus
UniProt:
  • Canonical: O70164 (Residues: 22-247; Coverage: 99%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYLKETONE INHIBITOR Chains: I, J
Molecule details ›
Chains: I, J
Length: 6 amino acids
Theoretical weight: 477 Da
Source organism: Mesocricetus auratus
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P43212
Unit cell:
a: 71.272Å b: 71.272Å c: 198.575Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.253
Expression systems:
  • unidentified baculovirus
  • Not provided

Quick links

Citations

3 review citations

Mast cell proteases as pharmacological targets.
Caughey GH. (2016)
2 more

1 mention without citation

Guinea pig chymase is leucine-specific: a novel example of functional plasticity in the chymase/granzyme family of serine peptidases.
Caughey et al. (2008)