› 2blv

X-ray diffraction
1.2Å resolution

Trypsin before a high dose x-ray "burn"

Released:
DOI: 10.2210/pdb2blv/pdb
PDB entry 2blv coloured by chain, front view.
PDB entry 2blv coloured by chain, side view.
PDB entry 2blv coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Improving radiation-damage substructures for RIP.
Nanao MH, Sheldrick GM, Ravelli RB
Acta Crystallogr D Biol Crystallogr 61 1227-37 (2005)
PMID: 16131756

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

4 bound ligands:
Ligand CA 1 x CA
Ligand BEN 1 x BEN
Ligand SO4 4 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 54.162Å b: 58.253Å c: 66.582Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.107 0.106 0.128

Quick links

Citations

2 review citations

Synergy within structural biology of single crystal optical spectroscopy and X-ray crystallography.
De la Mora-Rey et al. (2007)
1 more

6 mentions without citation

Identifying and quantifying radiation damage at the atomic level.
Gerstel et al. (2015)
5 more