› 1fxy

X-ray diffraction
2.15Å resolution

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

Released:
DOI: 10.2210/pdb1fxy/pdb
PDB entry 1fxy coloured by chain, front view.
PDB entry 1fxy coloured by chain, side view.
PDB entry 1fxy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
New enzyme lineages by subdomain shuffling.
Hopfner KP, Kopetzki E, Kresse GB, Bode W, Huber R, Engh RA
Proc Natl Acad Sci U S A 95 9813-8 (1998)
PMID: 9707558

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139600 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease 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
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand 0G6 1 x 0G6
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

Quick links

Citations

4 review citations

High-throughput screening of enzyme libraries.
Olsen et al. (2000)
3 more

3 mentions without citation

New enzyme lineages by subdomain shuffling.
Hopfner et al. (1998)
2 more