1edm

X-ray diffraction
1.5Å resolution

EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coagulation factor IXa light chain Chains: B, C
Molecule details ›
Chains: B, C
Length: 39 amino acids
Theoretical weight: 4.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00740 (Residues: 92-130; Coverage: 9%)
Gene name: F9
Sequence domains: EGF-like domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P43212
Unit cell:
a: 40.3Å b: 40.3Å c: 98.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.157 not available
Expression system: Escherichia coli