› 1cho

X-ray diffraction
1.8Å resolution

CRYSTAL AND MOLECULAR STRUCTURES OF THE COMPLEX OF ALPHA-*CHYMOTRYPSIN WITH ITS INHIBITOR TURKEY OVOMUCOID THIRD DOMAIN AT 1.8 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1cho/pdb
PDB entry 1cho coloured by chain, front view.
PDB entry 1cho coloured by chain, side view.
PDB entry 1cho coloured by chain, top view.
Source organisms:
Primary publication:
Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution.
Fujinaga M, Sielecki AR, Read RJ, Ardelt W, Laskowski M, James MN
J Mol Biol 195 397-418 (1987)
PMID: 3477645

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 domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133408 (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
Ovomucoid Chain: I
Molecule details ›
Chain: I
Length: 56 amino acids
Theoretical weight: 6.03 KDa
Source organism: Meleagris gallopavo
UniProt:
  • Canonical: P68390 (Residues: 130-185; Coverage: 30%)
Sequence domains: Kazal-type serine protease inhibitor domain
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 44.92Å b: 54.52Å c: 57.18Å
α: 90° β: 103.9° γ: 90°
R-values:
R R work R free
0.168 not available not available

Quick links

Citations

10 review citations

Natural protein proteinase inhibitors and their interaction with proteinases.
Bode et al. (1992)
9 more

48 mentions without citation

Anchor residues in protein-protein interactions.
Rajamani et al. (2004)
47 more