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Ligands
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FJD 3-[(3as,4r,5s,8as,8br)-4-[5-(5-chlorothiophen-2-yl)-1,3-oxazol-2-yl]-1,3-dioxo-4,6,7,8,8a,8b-hexahydro-3ah-pyrrolo[3,4-a]pyrrolizin-2-yl]propyl-trimethyl-azanium
NA Sodium ion
Non-standard Residues
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Glycosylation
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Modification
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Code : 2Y5G   PDBj   RCSB PDB   PDBe
Header : BLOOD CLOTTING
Title : FACTOR XA - CATION INHIBITOR COMPLEX
Release Data : 2011-12-28
Compound :
mol_id molecule chains synonym
1 ACTIVATED FACTOR XA HEAVY CHAIN A COAGULATION FACTOR XA
ec: 3.4.21.6
fragment: RESIDUES 235-468
mutation: YES
mol_id molecule chains synonym
2 FACTOR X LIGHT CHAIN L COAGULATION FACTOR XA
ec: 3.4.21.6
fragment: RESIDUES 127-180
Source :
mol_id organism_scientific organism_common expression_system
1 HOMO SAPIENS  (taxid:9606) HUMAN ESCHERICHIA COLI  (taxid:562)
mol_id organism_scientific organism_common expression_system
2 HOMO SAPIENS  (taxid:9606) HUMAN ESCHERICHIA COLI  (taxid:562)
Authors : Banner, D.W., Salonen, L.M., Holland, M.C., Haap, W., Benz, J., Diederich, F.
Keywords : BLOOD CLOTTING, PLASMA, ZYMOGEN, HYDROLASE, BLOOD COAGULATION, HYDROXYLATION, SERINE PROTEASE, EGF-LIKE DOMAIN
Exp. method : X-RAY DIFFRACTION ( 1.29 Å )
Citation :

Molecular Recognition at the Active Site of Factor Xa: Cation-Pi Interactions, Stacking on Planar Peptide Surfaces, and Replacement of Structural Water.

Salonen, L.M.,Holland, M.C.,Kaib, P.S.  et al.
(2012)  Chemistry  18 : 213

PubMed: 22162109
DOI: 10.1002/CHEM.201102571

Chain : L
UniProt : P00742 (FA10_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. 3.4.21.6 -
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