› 1tld

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.5 ANGSTROMS RESOLUTION IN A CRYSTAL FORM WITH LOW MOLECULAR PACKING DENSITY. ACTIVE SITE GEOMETRY, ION PAIRS AND SOLVENT STRUCTURE

Released:
DOI: 10.2210/pdb1tld/pdb
PDB entry 1tld coloured by chain, front view.
PDB entry 1tld coloured by chain, side view.
PDB entry 1tld coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure of bovine beta-trypsin at 1.5 A resolution in a crystal form with low molecular packing density. Active site geometry, ion pairs and solvent structure.
Bartunik HD, Summers LJ, Bartsch HH
J Mol Biol 210 813-28 (1989)
PMID: 2614845

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.32 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 63.7Å b: 63.5Å c: 68.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 not available

Quick links

Citations

7 review citations

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

6 mentions without citation

Structural basis for intramembrane proteolysis by rhomboid serine proteases.
Ben-Shem et al. (2007)
5 more