› 1f7e

Solution NMR

THE FIRST EGF-LIKE DOMAIN FROM HUMAN BLOOD COAGULATION FVII, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1f7e/pdb
PDB entry 1f7e coloured by chain, ensemble of 20 models, front view.
PDB entry 1f7e coloured by chain, ensemble of 20 models, side view.
PDB entry 1f7e coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The effect of O-fucosylation on the first EGF-like domain from human blood coagulation factor VII.
Kao YH, Lee GF, Wang Y, Starovasnik MA, Kelley RF, Spellman MW, Lerner L
Biochemistry 38 7097-110 (1999)
PMID: 10353820

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140350 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Factor VII light chain Chain: A
Molecule details ›
Chain: A
Length: 46 amino acids
Theoretical weight: 4.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08709 (Residues: 105-147; Coverage: 10%)
Gene name: F7
Sequence domains: EGF-like domain
Structure domains: Laminin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: HYBRID DISTANCE GEOMETRY - SIMULATED ANNEALING
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Fucose: biosynthesis and biological function in mammals.
Becker et al. (2003)
4 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)