2a31

X-ray diffraction
1.25Å resolution

Trypsin in complex with borate

Released:
Source organism: Sus scrofa

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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

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