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Magnesium in PDB 2yaz: The Crystal Structure of Leishmania Major Dutpase in Complex DumpEnzymatic activity of The Crystal Structure of Leishmania Major Dutpase in Complex Dump
All present enzymatic activity of The Crystal Structure of Leishmania Major Dutpase in Complex Dump:
3.6.1.23; Protein crystallography data
The structure of The Crystal Structure of Leishmania Major Dutpase in Complex Dump, PDB code: 2yaz
was solved by
G.R.Hemsworth,
O.V.Moroz,
M.J.Fogg,
B.Scott,
C.Bosch-Navarrete,
D.Gonzalez-Pacanowska,
K.S.Wilson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The Crystal Structure of Leishmania Major Dutpase in Complex Dump
(pdb code 2yaz). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the The Crystal Structure of Leishmania Major Dutpase in Complex Dump, PDB code: 2yaz: Jump to Magnesium binding site number: 1; 2; 3; Magnesium binding site 1 out of 3 in 2yazGo back to Magnesium Binding Sites List in 2yaz
Magnesium binding site 1 out
of 3 in the The Crystal Structure of Leishmania Major Dutpase in Complex Dump
Mono view Stereo pair view
Magnesium binding site 2 out of 3 in 2yazGo back to Magnesium Binding Sites List in 2yaz
Magnesium binding site 2 out
of 3 in the The Crystal Structure of Leishmania Major Dutpase in Complex Dump
Mono view Stereo pair view
Magnesium binding site 3 out of 3 in 2yazGo back to Magnesium Binding Sites List in 2yaz
Magnesium binding site 3 out
of 3 in the The Crystal Structure of Leishmania Major Dutpase in Complex Dump
Mono view Stereo pair view
Reference:
G.R.Hemsworth,
O.V.Moroz,
M.J.Fogg,
B.Scott,
C.Bosch-Navarrete,
D.Gonzalez-Pacanowska,
K.S.Wilson.
The Crystal Structure of the Leishmania Major Deoxyuridine Triphosphate Nucleotidohydrolase in Complex with Nucleotide Analogues, Dump, and Deoxyuridine. J.Biol.Chem. V. 286 16470 2011.
Page generated: Mon Dec 14 07:48:33 2020
ISSN: ISSN 0021-9258 PubMed: 21454646 DOI: 10.1074/JBC.M111.224873 |
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