X-ray diffraction
1.1Å resolution

Crystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, cryo temperature

Source organism: Bos taurus
Entry authors: Kreinbring CA, Wilson MA, Kovalevsky AY, Blakeley MP, Fisher SZ, Lazar LM, Moulin AG, Novak WR, Petsko GA, Ringe D

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
Chymotrypsin A chain A Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Bos taurus
  • 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
  • Canonical: P00766 (Residues: 16-146; Coverage: 54%)
Chymotrypsin A chain C Chain: C
Molecule details ›
Chain: C
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
peptide SWPW Chain: D
Molecule details ›
Chain: D
Length: 4 amino acids
Theoretical weight: 575 Da
Source organism: Bos taurus
peptide TPGVY Chain: E
Molecule details ›
Chain: E
Length: 5 amino acids
Theoretical weight: 536 Da
Source organism: Bos taurus

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P42212
Unit cell:
a: 68.525Å b: 68.525Å c: 96.685Å
α: 90° β: 90° γ: 90°
R R work R free
0.12 0.119 0.131