› 1try

X-ray diffraction
1.55Å resolution

STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS

Released:
DOI: 10.2210/pdb1try/pdb
PDB entry 1try coloured by chain, front view.
PDB entry 1try coloured by chain, side view.
PDB entry 1try coloured by chain, top view.
Source organism: Fusarium oxysporum
Primary publication:
Structure of inhibited trypsin from Fusarium oxysporum at 1.55 A.
Rypniewski WR, Dambmann C, von der Osten C, Dauter M, Wilson KS
Acta Crystallogr D Biol Crystallogr 51 73-85 (1995)
PMID: 15299338

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

2 bound ligands:
Ligand ISP 1 x ISP
Ligand IPA 1 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 33.3Å b: 67.89Å c: 39.79Å
α: 90° β: 107.33° γ: 90°
R-values:
R R work R free
0.144 not available not available

Quick links

Citations

2 citation in other articles

The crystal structure of the Epstein-Barr virus protease shows rearrangement of the processed C terminus.
Buisson et al. (2002)
1 more

1 mention without citation

Modeling and structural analysis of PA clan serine proteases.
Laskar et al. (2012)