› 2a31

X-ray diffraction
1.25Å resolution

Trypsin in complex with borate

Released:
DOI: 10.2210/pdb2a31/pdb
PDB entry 2a31 coloured by chain, front view.
PDB entry 2a31 coloured by chain, side view.
PDB entry 2a31 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
NMR and crystallographic characterization of adventitious borate binding by trypsin.
Transue TR, Gabel SA, London RE
Bioconjug Chem 17 300-8
PMID: 16536459

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-133375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypsin Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 23.49 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P00761 (Residues: 9-231; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

6 bound ligands:
Ligand CA 1 x CA
Ligand MG 3 x MG
Ligand NA 1 x NA
Ligand SO4 1 x SO4
Ligand BO4 2 x BO4
Ligand PG3 1 x PG3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 76.304Å b: 53.446Å c: 46.466Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.14 0.162

Quick links

Citations

1 review citation

Boron-containing compounds: chemico-biological properties and expanding medicinal potential in prevention, diagnosis and therapy.
Soriano-Ursúa et al. (2014)
7 other articles

9 mentions without citation

Predicting the accuracy of protein-ligand docking on homology models.
Bordogna et al. (2011)
8 more