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Atomistry » Calcium » PDB 2hih-2i52 » 2hih | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 2hih-2i52 » 2hih » |
Calcium in PDB 2hih: Crystal Structure of Staphylococcus Hyicus LipaseEnzymatic activity of Crystal Structure of Staphylococcus Hyicus Lipase
All present enzymatic activity of Crystal Structure of Staphylococcus Hyicus Lipase:
3.1.1.3; Protein crystallography data
The structure of Crystal Structure of Staphylococcus Hyicus Lipase, PDB code: 2hih
was solved by
J.J.W.Tiesinga,
G.Van Pouderoyen,
M.Nardini,
B.W.Dijkstra,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2hih:
The structure of Crystal Structure of Staphylococcus Hyicus Lipase also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Staphylococcus Hyicus Lipase
(pdb code 2hih). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Staphylococcus Hyicus Lipase, PDB code: 2hih: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 2hihGo back to Calcium Binding Sites List in 2hih
Calcium binding site 1 out
of 2 in the Crystal Structure of Staphylococcus Hyicus Lipase
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 2hihGo back to Calcium Binding Sites List in 2hih
Calcium binding site 2 out
of 2 in the Crystal Structure of Staphylococcus Hyicus Lipase
Mono view Stereo pair view
Reference:
J.J.Tiesinga,
G.Van Pouderoyen,
M.Nardini,
S.Ransac,
B.W.Dijkstra.
Structural Basis of Phospholipase Activity of Staphylococcus Hyicus Lipase. J.Mol.Biol. V. 371 447 2007.
Page generated: Sat Dec 12 03:39:18 2020
ISSN: ISSN 0022-2836 PubMed: 17582438 DOI: 10.1016/J.JMB.2007.05.041 |
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