› 2cga

X-ray diffraction
1.8Å resolution

BOVINE CHYMOTRYPSINOGEN A. X-RAY CRYSTAL STRUCTURE ANALYSIS AND REFINEMENT OF A NEW CRYSTAL FORM AT 1.8 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2cga/pdb
PDB entry 2cga coloured by chain, front view.
PDB entry 2cga coloured by chain, side view.
PDB entry 2cga coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution.
Wang D, Bode W, Huber R
J Mol Biol 185 595-624 (1985)
PMID: 4057257

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chymotrypsinogen A Chains: A, B
Molecule details ›
Chains: A, B
Length: 245 amino acids
Theoretical weight: 25.69 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00766 (Residues: 1-245; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 59.3Å b: 77.1Å c: 110.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 not available
Expression system: Not provided

Quick links

Citations

11 review citations

Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
Khan et al. (1998)
10 more

39 mentions without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)
38 more