› 4pti

X-ray diffraction
1.5Å resolution

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

Released:
DOI: 10.2210/pdb4pti/pdb
PDB entry 4pti coloured by chain, front view.
PDB entry 4pti coloured by chain, side view.
PDB entry 4pti coloured by chain, top view.
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

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133749 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic trypsin inhibitor Chain: A
Molecule details ›
Chain: A
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 43.1Å b: 22.9Å c: 48.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.162 not available
Expression system: Not provided

Quick links

Citations

37 mentions without citation

Clustering of low-energy conformations near the native structures of small proteins.
Shortle et al. (1998)
36 more