PDBe 1fxy

X-ray diffraction
2.15Å resolution

COAGULATION FACTOR XA-TRYPSIN CHIMERA INHIBITED WITH D-PHE-PRO-ARG-CHLOROMETHYLKETONE

Released:
Source organism: Homo sapiens
Primary publication:
New enzyme lineages by subdomain shuffling.
Proc. Natl. Acad. Sci. U.S.A. 95 9813-8 (1998)
PMID: 9707558

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypsin-1 Chain: A
Molecule details ›
Chain: A
Length: 228 amino acids
Theoretical weight: 24.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07477 (Residues: 24-41, 42-64, 65-67, 68-247; Coverage: 96%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 65.51Å b: 48.92Å c: 75.54Å
α: 90° β: 111.46° γ: 90°
R-values:
R R work R free
0.18 0.18 0.245
Expression system: Escherichia coli