2wpl

X-ray diffraction
1.82Å resolution

factor IXa superactive triple mutant, EDTA-soaked

Released:

Function and Biology Details

Reaction catalysed:
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Coagulation factor IXa light chain Chain: E
Molecule details ›
Chain: E
Length: 59 amino acids
Theoretical weight: 6.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00740 (Residues: 133-191; Coverage: 14%)
Gene name: F9
Sequence domains: Coagulation Factor Xa inhibitory site
Structure domains: Laminin
D-PHE-PRO-ARG-CHLOROMETHYL KETONE Chain: L
Molecule details ›
Chain: L
Length: 3 amino acids
Theoretical weight: 419 Da
Source organism: synthetic construct
Expression system: Not provided
Coagulation factor IXa heavy chain Chain: S
Molecule details ›
Chain: S
Length: 235 amino acids
Theoretical weight: 26.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00740 (Residues: 227-461; Coverage: 54%)
Gene name: F9
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 44.42Å b: 66.71Å c: 98.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.289
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided