4bdx

X-ray diffraction
1.62Å resolution

The structure of the FnI-EGF tandem domain of coagulation factor XII

Released:
Source organism: Homo sapiens
Primary publication:
The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 94-102 (2013)
PMID: 23385745

Function and Biology Details

Reaction catalysed:
Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coagulation factor XIIa heavy chain Chain: A
Molecule details ›
Chain: A
Length: 85 amino acids
Theoretical weight: 9.54 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P00748 (Residues: 133-215; Coverage: 14%)
Gene name: F12
Sequence domains:
Structure domains: Laminin

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I4122
Unit cell:
a: 96.788Å b: 96.788Å c: 47.477Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.216 0.247
Expression system: Komagataella pastoris