› 2pf2

X-ray diffraction
2.2Å resolution

THE CA+2 ION AND MEMBRANE BINDING STRUCTURE OF THE GLA DOMAIN OF CA-PROTHROMBIN FRAGMENT 1

Released:
DOI: 10.2210/pdb2pf2/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 2pf2 coloured by chain, front view.
PDB entry 2pf2 coloured by chain, side view.
PDB entry 2pf2 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1.
Soriano-Garcia M, Padmanabhan K, de Vos AM, Tulinsky A
Biochemistry 31 2554-66 (1992)
PMID: 1547238

Function and Biology Details

Reaction catalysed: 
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Activation peptide fragment 1 Chain: A
Molecule details ›
Chain: A
Length: 156 amino acids
Theoretical weight: 18.02 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00735 (Residues: 44-199; Coverage: 26%)
Gene name: F2
Sequence domains:
Structure domains: Plasminogen Kringle 4

Ligands and Environments

1 bound ligand:
Ligand CA 7 x CA
1 modified residue:
Ligand CGU 10 x CGU

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P212121
Unit cell:
a: 39.39Å b: 53.88Å c: 129.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 not available not available
Expression system: Not provided

Quick links

Citations

24 review citations

A player of many parts: the spotlight falls on thrombin's structure.
Stubbs et al. (1993)
23 more

1 mention without citation

Face-specific binding of prothrombin fragment 1 and human serum albumin to inorganic and urinary calcium oxalate monohydrate crystals.
Cook et al. (2009)