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Literature summary for 3.4.21.6 extracted from

  • Venkateswarlu, D.; Perera, L.; Darden, T.; Pedersen, L.G.
    Structure and dynamics of zymogen human blood coagulation factor X (2002), Biophys. J., 82, 1190-1206.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.6

Activating Compound

Activating Compound Comment Organism Structure
Phospholipids interaction via Lys14 of the Gla-domain Homo sapiens

Protein Variants

Protein Variants Comment Organism
G114R simulation of the exchange of residues, conserved residue in the EGF2 domain sulfide loop, disruptive salt bridge interaction or blockage of interaction with factors VIIIa/IXa Homo sapiens
G323S simulation of the exchange of residues, mutation disrupts a highly conserved beta-sheet structure Homo sapiens
N57T simulation of the exchange of residues, loss of interaction with Cys81 with structural implications Homo sapiens
P343S simulation of the exchange of residues, conserved residue involved in a suface beta-sheet, affects intrinsic folding Homo sapiens
R326C simulation of the exchange of residues, surface residue, involved in protein-protein interactions, interaction with Gln376 located in the S1-binding site Homo sapiens
T318M simulation of the exchange of residues, surface residue involved in a side-chain hydrogen bond with Glu341 which is lost in the mutant, leads to clinical effect Homo sapiens
V298M simulation of the exchange of residues, unfolding occurs due to space limitation Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on, required for coordination of the enzyme domains, residues Asp46, Gly47, Gln49, and Gly64 are involved in Ca2+ binding, modeling of the calcium-binding site within the serine protease domain Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00742
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification reorientation of the N-terminus of serine protease domain after proteolytic activation of factor X to factor Xa, cleavage of the activation peptide at the Arg194-Ile195 peptide bond Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
selective cleavage of Arg-/-Thr and then Arg-/-Ile bonds in prothrombin to form thrombin scutelarin has similar specificity Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prothrombin + H2O
-
 Homo sapiens thrombin + ?
-
 ?

Subunits

Subunits Comment Organism
More schematic representation and modeling of the structure of the two peptide chains of factor X, amino acid sequence, enzyme possesses an activation peptide, a catalytic serine protease domain, a GF2 domain, and a EGF1 domain, overview Homo sapiens

Synonyms

Synonyms Comment Organism
blood coagulation factor X zymogen Homo sapiens
factor Xa mature enzyme Homo sapiens
fX
-
 Homo sapiens
FXa
-
 Homo sapiens
More the enzyme belongs to the peptidase family S1, i.e. trypsin family Homo sapiens

Cofactor

Cofactor Comment Organism Structure
vitamin K dependent on Homo sapiens