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Ligands
Code Name Style Show Link
CA Calcium ion
MG Magnesium ion
Non-standard Residues
Code Name Show
CGU Gamma-carboxy-glutamic acid
Glycosylation
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Modification
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Code : 1J34   PDBj   RCSB PDB   PDBe
Header : Protein binding/Blood clotting
Title : Crystal Structure of Mg(II)-and Ca(II)-bound Gla Domain of Factor IX Complexed with Binding Protein
Release Data : 2003-07-08
Compound :
mol_id molecule chains synonym
1 coagulation factor IX-binding protein A chain A COAGULATION FACTOR IX BINDING PROTEIN CHAIN A
mol_id molecule chains
2 coagulation factor IX-binding protein B chain B
mol_id molecule chains
3 Coagulation factor IX C
ec: 3.4.21.22
fragment: GLA DOMAIN
Source :
mol_id organism_scientific
1 Trimeresurus flavoviridis  (taxid:88087)
secretion: venom
mol_id organism_scientific
2 Trimeresurus flavoviridis  (taxid:88087)
secretion: venom
mol_id organism_scientific organism_common
3 Bos taurus  (taxid:9913) Cattle
secretion: plasma
Authors : Shikamoto, Y., Morita, T., Fujimoto, Z., Mizuno, H.
Keywords : MAGNESIUM ION, CALCIUM ION, GLA DOMAIN, Protein binding-Blood clotting COMPLEX
Exp. method : X-RAY DIFFRACTION ( 1.55 Å )
Citation :

Crystal Structure of Mg2+- and Ca2+-bound Gla Domain of Factor IX Complexed with Binding Protein

Shikamoto, Y.,Morita, T.,Fujimoto, Z.  et al.
(2003)  J.Biol.Chem.  278 : 24090 - 24094

PubMed: 12695512
DOI: 10.1074/jbc.M300650200

Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X

Mizuno, H.,Fujimoto, Z.,Atoda, H.  et al.
(2001)  Proc.Natl.Acad.Sci.USA  98 : 7230 - 7234

DOI: 10.1073/pnas.131179698

Crystal structure of coagulation factor IX-binding protein from habu snake venom at 2.6 A: implication of central loop swapping based on deletion in the linker region

Mizuno, H.,Fujimoto, Z.,Koizumi, M.  et al.
(1999)  J.Mol.Biol.  289 : 103 - 112

DOI: 10.1006/jmbi.1999.2756

Chain : A
UniProt : P23806 (SL9A_PROFL)
Reaction : -
Chain : B
UniProt : P23807 (SL9B_PROFL)
Reaction : -
Chain : C
UniProt : P00741 (FA9_BOVIN)
Reaction: EC: Evidence:
Physiological Direction:
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa. 3.4.21.22 PubMed:6782101
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