› 1mgx

Solution NMR

COAGULATION FACTOR, MG(II), NMR, 7 STRUCTURES (BACKBONE ATOMS ONLY)

Released:
DOI: 10.2210/pdb1mgx/pdb
PDB entry 1mgx coloured by chain, ensemble of 7 models, front view.
PDB entry 1mgx coloured by chain, ensemble of 7 models, side view.
PDB entry 1mgx coloured by chain, ensemble of 7 models, top view.
Source organism: Homo sapiens
Primary publication:
Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX.
Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B
J Biol Chem 271 16227-36 (1996)
PMID: 8663165

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: 6.29 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

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CGU 12 x CGU

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

8 review citations

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

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)