› 2g51

X-ray diffraction
1.84Å resolution

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-152777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypsin Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 22.2 KDa
Source organism: Fusarium oxysporum
UniProt:
  • Canonical: P35049 (Residues: 25-248; Coverage: 97%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P1
Unit cell:
a: 32.9Å b: 36.8Å c: 39.63Å
α: 102.46° β: 104.97° γ: 102.16°
R-values:
R R work R free
0.161 0.16 0.216

Quick links

Citations

4 review citations

Conformational selection in trypsin-like proteases.
Pozzi et al. (2012)
3 more

2 mentions without citation

Allostery in trypsin-like proteases suggests new therapeutic strategies.
Gohara et al. (2011)
1 more