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Atomistry » Calcium » PDB 1dva-1edh » 1e7y » |
Calcium in PDB 1e7y: Active Site Mutant (D177->N) of Glucose 6-Phosphate Dehydrogenase From Leuconostoc Mesenteroides Complexed with Substrate and NadphEnzymatic activity of Active Site Mutant (D177->N) of Glucose 6-Phosphate Dehydrogenase From Leuconostoc Mesenteroides Complexed with Substrate and Nadph
All present enzymatic activity of Active Site Mutant (D177->N) of Glucose 6-Phosphate Dehydrogenase From Leuconostoc Mesenteroides Complexed with Substrate and Nadph:
1.1.1.49; Protein crystallography data
The structure of Active Site Mutant (D177->N) of Glucose 6-Phosphate Dehydrogenase From Leuconostoc Mesenteroides Complexed with Substrate and Nadph, PDB code: 1e7y
was solved by
M.J.Adams,
M.S.Cosgrove,
S.Gover,
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 Active Site Mutant (D177->N) of Glucose 6-Phosphate Dehydrogenase From Leuconostoc Mesenteroides Complexed with Substrate and Nadph
(pdb code 1e7y). 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 Active Site Mutant (D177->N) of Glucose 6-Phosphate Dehydrogenase From Leuconostoc Mesenteroides Complexed with Substrate and Nadph, PDB code: 1e7y: Calcium binding site 1 out of 1 in 1e7yGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Active Site Mutant (D177->N) of Glucose 6-Phosphate Dehydrogenase From Leuconostoc Mesenteroides Complexed with Substrate and Nadph
![]() Mono view ![]() Stereo pair view
Reference:
M.S.Cosgrove,
S.Gover,
C.E.Naylor,
L.Vandeputte-Rutten,
M.J.Adams,
H.R.Levy.
An Examination of the Role of Asp-177 in the His-Asp Catalytic Dyad of Leuconostoc Mesenteroides Glucose 6-Phosphate Dehydrogenase: X-Ray Structure and pH Dependence of Kinetic Parameters of the D177N Mutant Enzyme Biochemistry V. 39 15002 2000.
Page generated: Mon Jul 7 14:35:26 2025
ISSN: ISSN 0006-2960 PubMed: 11106478 DOI: 10.1021/BI0014608 |
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