› 6di8

X-ray diffraction
1.86Å resolution

Crystal structure of bovine alpha-chymotrypsin in space group P65

Released:
DOI: 10.2210/pdb6di8/pdb
Model geometry
Fit model/data
PDB entry 6di8 coloured by chain, front view.
PDB entry 6di8 coloured by chain, side view.
PDB entry 6di8 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal Structure of Bovine Alpha-Chymotrypsin in Space Group P65
Marshall AC, Keiller BG, Pederick JL, Abell AD, Bruning JB
Crystals 8 460-466 (2018)

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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133405 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chymotrypsin A chain A Chains: A, D, G, J
Molecule details ›
Chains: A, D, G, J
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: B, E, H, K
Molecule details ›
Chains: B, E, H, K
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: C, F, I, L

Ligands and Environments

1 bound ligand:
Ligand SO4 13 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P65
Unit cell:
a: 126.81Å b: 126.81Å c: 122.03Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.225

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