2vvc

X-ray diffraction
1.95Å resolution

Aminopyrrolidine Factor Xa inhibitor

Released:

Function and Biology Details

Reaction catalysed:
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Activated factor Xa heavy chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 241 amino acids
Theoretical weight: 27.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00742 (Residues: 235-475; Coverage: 53%)
Gene name: F10
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Factor X light chain Chains: K, L
Molecule details ›
Chains: K, L
Length: 55 amino acids
Theoretical weight: 6.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00742 (Residues: 126-180; Coverage: 12%)
Gene name: F10
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21
Unit cell:
a: 48.96Å b: 77.19Å c: 74.76Å
α: 90° β: 92.12° γ: 90°
R-values:
R R work R free
0.203 0.199 0.275
Expression system: Escherichia coli