1klt

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF PMSF-TREATED HUMAN CHYMASE AT 1.9 ANGSTROMS RESOLUTION

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Phe-|- > Tyr-|- > Trp-|- > Leu-|-.
Biochemical function:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chymase Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 25.05 KDa
Source organism: Homo sapiens
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P23946 (Residues: 22-247; Coverage: 99%)
  • Best match: P23946-2 (Residues: 1-136)
Gene names: CMA1, CYH, CYM
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 43.93Å b: 58.16Å c: 86.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.255
Expression system: Bacillus subtilis