› 4ag2

X-ray diffraction
1.8Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150132 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chymase Chains: A, B
Molecule details ›
Chains: A, B
Length: 226 amino acids
Theoretical weight: 25.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23946 (Residues: 22-247; Coverage: 99%)
Gene names: CMA1, CYH, CYM
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
FYNOMER Chains: C, D
Molecule details ›
Chains: C, D
Length: 84 amino acids
Theoretical weight: 9.61 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: SH3 Domains

Ligands and Environments

3 bound ligands:
Ligand MES 2 x MES
Ligand LMR 3 x LMR
Ligand NA 5 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 56.937Å b: 64.124Å c: 174.987Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.212
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Challenges and opportunities for non-antibody scaffold drugs.
Vazquez-Lombardi et al. (2015)
8 more

2 mentions without citation

Generation, characterization and structural data of chymase binding proteins based on the human Fyn kinase SH3 domain.
Schlatter et al. (2012)
1 more