› 1tpa

X-ray diffraction
1.9Å resolution

THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS

Released:
DOI: 10.2210/pdb1tpa/pdb
PDB 1tpa coloured by chain and viewed from the front.
PDB 1tpa coloured by chain and viewed from the side.
PDB 1tpa coloured by chain and viewed from the top.
Source organism: Bos taurus
Primary publication:
The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors
Marquart M, Walter J, Deisenhofer J, Bode W, Huber R
Acta Crystallogr., B 39 480- (1983)

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero octamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cationic trypsin Chain: E
Molecule details ›
Chain: E
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Pancreatic trypsin inhibitor Chain: I
Molecule details ›
Chain: I
Length: 58 amino acids
Theoretical weight: 6.53 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00974 (Residues: 36-93; Coverage: 73%)
Sequence domains: Kunitz/Bovine pancreatic trypsin inhibitor domain
Structure domains: Pancreatic trypsin inhibitor Kunitz domain

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 75.5Å b: 84.4Å c: 122.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 not available
Expression system: Not provided

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Citations

4 mentions without citation

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