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Literature summary for extracted from

  • Johnson, D.J.; Langdown, J.; Huntington, J.A.
    Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex (2010), Proc. Natl. Acad. Sci. USA, 107, 645-650.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Factor VIIIa
Homo sapiens


Cloned (Comment) Organism
expressed in Escherichia coli BL21 Star (DE3) cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 0.25 M ammonium acetate, 19.5% (w/v) PEG 3350 Homo sapiens


Inhibitors Comment Organism Structure
Homo sapiens


Metals/Ions Comment Organism Structure
Ca2+ factor IXa contains a high-affinity Ca2+-binding site Homo sapiens
additional information factor IXa is not a Na+-binding protease Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Factor X + H2O Homo sapiens
Factor Xa + ?


Organism UniProt Comment Textmining
Homo sapiens P00740

Purification (Commentary)

Purification (Comment) Organism
heparin Sepharose column chromatography and Q Sepharose column chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Factor X + H2O
Homo sapiens Factor Xa + ?


Synonyms Comment Organism
factor IXa
Homo sapiens
Homo sapiens

General Information

General Information Comment Organism
malfunction factor IXa deficiency results in hemophilia Homo sapiens
physiological function factor IXa is a critical enzyme for the formation of stable blood clots Homo sapiens