1j17

X-ray diffraction
2Å resolution

FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH RAT TRYPSIN MUTANT X99/175/190RT

Released:

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:
Anionic trypsin-2 Chain: T
Molecule details ›
Chain: T
Length: 223 amino acids
Theoretical weight: 23.84 KDa
Source organism: Rattus norvegicus
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00763 (Residues: 24-246; Coverage: 97%)
Gene names: Prss2, Try2
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: I23
Unit cell:
a: 124.78Å b: 124.78Å c: 124.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 not available
Expression system: Saccharomyces cerevisiae