6b77

X-ray diffraction
2.37Å resolution

Structures of the two-chain human plasma factor XIIa co-crystallized with potent inhibitors

Released:

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:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-133244 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Beta-factor XIIa part 1 Chain: A
Molecule details ›
Chain: A
Length: 9 amino acids
Theoretical weight: 932 Da
Source organism: Homo sapiens
UniProt:
  • Canonical: P00748 (Residues: 354-362; Coverage: 2%)
Gene name: F12
Coagulation factor XIIa light chain Chain: B
Molecule details ›
Chain: B
Length: 243 amino acids
Theoretical weight: 26.13 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P00748 (Residues: 373-615; Coverage: 41%)
Gene name: F12
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: I41
Unit cell:
a: 79.402Å b: 79.402Å c: 122.246Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 0.218