1gct

X-ray diffraction
1.6Å resolution

IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?

Released:
Source organism: Bos taurus
Primary publication:
Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?
Biochemistry 28 7033-8 (1989)
PMID: 2819046

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-524240 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Chymotrypsin A chain A Chain: A
Molecule details ›
Chain: A
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: B
Molecule details ›
Chain: B
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: C
Molecule details ›
Chain: C
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
TETRAPEPTIDE ADDUCT Chain: D
Molecule details ›
Chain: D
Length: 5 amino acids
Theoretical weight: 492 Da

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P42212
Unit cell:
a: 69.8Å b: 69.8Å c: 98.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 not available