› 2bya

X-ray diffraction
1.3Å resolution

Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection

Released:
DOI: 10.2210/pdb2bya/pdb
PDB entry 2bya coloured by chain, front view.
PDB entry 2bya coloured by chain, side view.
PDB entry 2bya coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?
Leiros HK, Timmins J, Ravelli RB, McSweeney SM
Acta Crystallogr D Biol Crystallogr 62 125-32 (2006)
PMID: 16421442

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
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: X
Molecule details ›
Chain: X
Length: 243 amino acids
Theoretical weight: 25.44 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00760 (Residues: 4-246; Coverage: 100%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 54.274Å b: 58.359Å c: 66.782Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.109 0.108 0.142

Quick links

Citations

3 review citations

Bacteriorhodopsin: Would the real structural intermediates please stand up?
Wickstrand et al. (2015)
2 more

2 mentions without citation

Peptides Isolated from Amphibian Skin Secretions with Emphasis on Antimicrobial Peptides.
Chen et al. (2022)
1 more