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Atomistry » Calcium » PDB 1i73-1iqi » 1ika » |
Calcium in PDB 1ika: Structure of Isocitrate Dehydrogenase with Alpha-Ketoglutarate at 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation of IsocitrateEnzymatic activity of Structure of Isocitrate Dehydrogenase with Alpha-Ketoglutarate at 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation of Isocitrate
All present enzymatic activity of Structure of Isocitrate Dehydrogenase with Alpha-Ketoglutarate at 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation of Isocitrate:
1.1.1.42; Protein crystallography data
The structure of Structure of Isocitrate Dehydrogenase with Alpha-Ketoglutarate at 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation of Isocitrate, PDB code: 1ika
was solved by
B.L.Stoddard,
D.E.Koshland Junior,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of Isocitrate Dehydrogenase with Alpha-Ketoglutarate at 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation of Isocitrate
(pdb code 1ika). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Isocitrate Dehydrogenase with Alpha-Ketoglutarate at 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation of Isocitrate, PDB code: 1ika: Calcium binding site 1 out of 1 in 1ikaGo back to Calcium Binding Sites List in 1ika
Calcium binding site 1 out
of 1 in the Structure of Isocitrate Dehydrogenase with Alpha-Ketoglutarate at 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation of Isocitrate
Mono view Stereo pair view
Reference:
B.L.Stoddard,
D.E.Koshland Jr..
Structure of Isocitrate Dehydrogenase with Alpha-Ketoglutarate at 2.7-A Resolution: Conformational Changes Induced By Decarboxylation of Isocitrate. Biochemistry V. 32 9317 1993.
Page generated: Thu Jul 11 10:20:52 2024
ISSN: ISSN 0006-2960 PubMed: 8369301 DOI: 10.1021/BI00087A009 |
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