1gmd

X-ray diffraction
2.2Å resolution

X-ray crystal structure of gamma-chymotrypsin in hexane

Released:
Source organism: Bos taurus
Primary publication:
X-ray crystal structure of gamma-chymotrypsin in hexane.
Biochemistry 33 7326-36 (1994)
PMID: 8003497

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
PDBe Complex ID:
PDB-CPX-133443 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Chymotrypsin A chain A Chain: E
Molecule details ›
Chain: E
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-13; Coverage: 5%)
Chymotrypsin A chain B Chain: F
Molecule details ›
Chain: F
Length: 131 amino acids
Theoretical weight: 13.93 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 16-146; Coverage: 54%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Chymotrypsin A chain C Chain: G
Molecule details ›
Chain: G
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
PRO GLY ALA TYR ASP PEPTIDE Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 522 Da
Source organism: Bos taurus

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P42212
Unit cell:
a: 69.34Å b: 69.32Å c: 97.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available