1ghb

X-ray diffraction
2Å resolution

A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN

Released:
Source organism: Bos taurus

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

Assemblies composition:
hetero octamer
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-133411 (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 Chain: P
Molecule details ›
Chain: P
Length: 3 amino acids
Theoretical weight: 243 Da

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P42212
Unit cell:
a: 69.6Å b: 69.6Å c: 97.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.152 not available