› 1cfh

Solution NMR

STRUCTURE OF THE METAL-FREE GAMMA-CARBOXYGLUTAMIC ACID-RICH MEMBRANE BINDING REGION OF FACTOR IX BY TWO-DIMENSIONAL NMR SPECTROSCOPY

Released:
DOI: 10.2210/pdb1cfh/pdb
PDB entry 1cfh coloured by chain, ensemble of 15 models, front view.
PDB entry 1cfh coloured by chain, ensemble of 15 models, side view.
PDB entry 1cfh coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
Freedman SJ, Furie BC, Furie B, Baleja JD
J Biol Chem 270 7980-7 (1995)
PMID: 7713897

Function and Biology Details

Reaction catalysed: 
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133190 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coagulation factor IXa light chain Chain: A
Molecule details ›
Chain: A
Length: 47 amino acids
Theoretical weight: 5.77 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00740 (Residues: 47-93; Coverage: 11%)
Gene name: F9
Sequence domains: Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain
Structure domains: Coagulation Factor IX

Ligands and Environments

1 bound ligand:
Ligand FMT 12 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

4 review citations

Lipid-protein interactions in blood coagulation.
Zwaal et al. (1998)
3 more

3 mentions without citation

Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.
Bah et al. (2016)
2 more