› 1yph

X-ray diffraction
1.34Å resolution

High resolution structure of bovine alpha-chymotrypsin

Released:
DOI: 10.2210/pdb1yph/pdb
PDB entry 1yph coloured by chain, front view.
PDB entry 1yph coloured by chain, side view.
PDB entry 1yph coloured by chain, top view.
Source organism: Bos taurus
Entry authors: Razeto A, Galunsky B, Kasche V, Wilson KS, Lamzin VS

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133435 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chymotrypsin A chain A Chains: A, B
Molecule details ›
Chains: A, B
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 Chains: C, D
Molecule details ›
Chains: C, D
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 Chains: E, F
Molecule details ›
Chains: E, F
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

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 43.83Å b: 77.51Å c: 62.77Å
α: 90° β: 106.3° γ: 90°
R-values:
R R work R free
0.139 0.139 0.189

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