4xde

X-ray diffraction
2.14Å resolution

Coagulation Factor XII protease domain crystal structure

Released:
Source organism: Homo sapiens

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coagulation factor XIIa light chain Chain: A
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 27.88 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: P00748 (Residues: 373-615; Coverage: 41%)
Gene name: F12
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P41212
Unit cell:
a: 124.126Å b: 124.126Å c: 38.145Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.262
Expression system: Drosophila melanogaster