› 1apo

Solution NMR

THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE N-TERMINAL EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X AS DETERMINED BY NMR SPECTROSCOPY AND SIMULATED FOLDING

Released:
DOI: 10.2210/pdb1apo/pdb
PDB entry 1apo coloured by chain, ensemble of 13 models, front view.
PDB entry 1apo coloured by chain, ensemble of 13 models, side view.
PDB entry 1apo coloured by chain, ensemble of 13 models, top view.
Source organism: Bos taurus
Primary publication:
Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding.
Ullner M, Selander M, Persson E, Stenflo J, Drakenberg T, Teleman O
Biochemistry 31 5974-83 (1992)
PMID: 1627540

Function and Biology Details

Reaction catalysed: 
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
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-133220 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Factor X light chain Chain: A
Molecule details ›
Chain: A
Length: 42 amino acids
Theoretical weight: 4.56 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00743 (Residues: 85-126; Coverage: 9%)
Gene name: F10
Sequence domains: EGF-like domain
Structure domains: Laminin

Ligands and Environments

1 bound ligand:
Ligand OH 1 x OH
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

6 review citations

Exposure of platelet membrane phosphatidylserine regulates blood coagulation.
Lentz BR. (2003)
5 more

4 mentions without citation

Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field.
Nielsen et al. (2012)
3 more