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Atomistry » Calcium » PDB 1edm-1evu » 1eth | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 1edm-1evu » 1eth » |
Calcium in PDB 1eth: Triacylglycerol Lipase/Colipase ComplexEnzymatic activity of Triacylglycerol Lipase/Colipase Complex
All present enzymatic activity of Triacylglycerol Lipase/Colipase Complex:
3.1.1.3; Protein crystallography data
The structure of Triacylglycerol Lipase/Colipase Complex, PDB code: 1eth
was solved by
J.Hermoso,
D.Pignol,
B.Kerfelec,
I.Crenon,
C.Chapus,
J.C.Fontecilla-Camps,
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 Triacylglycerol Lipase/Colipase Complex
(pdb code 1eth). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Triacylglycerol Lipase/Colipase Complex, PDB code: 1eth: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1ethGo back to Calcium Binding Sites List in 1eth
Calcium binding site 1 out
of 2 in the Triacylglycerol Lipase/Colipase Complex
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 1ethGo back to Calcium Binding Sites List in 1eth
Calcium binding site 2 out
of 2 in the Triacylglycerol Lipase/Colipase Complex
Mono view Stereo pair view
Reference:
J.Hermoso,
D.Pignol,
B.Kerfelec,
I.Crenon,
C.Chapus,
J.C.Fontecilla-Camps.
Lipase Activation By Nonionic Detergents. the Crystal Structure of the Porcine Lipase-Colipase-Tetraethylene Glycol Monooctyl Ether Complex. J.Biol.Chem. V. 271 18007 1996.
Page generated: Thu Jul 11 07:57:06 2024
ISSN: ISSN 0021-9258 PubMed: 8663362 DOI: 10.1074/JBC.271.30.18007 |
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