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Atomistry » Magnesium » PDB 1x1t-1xfx » 1xbx | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1x1t-1xfx » 1xbx » |
Magnesium in PDB 1xbx: Structure of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase E112D/R139V/T169A Mutant with Bound D-Ribulose 5-PhosphateProtein crystallography data
The structure of Structure of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase E112D/R139V/T169A Mutant with Bound D-Ribulose 5-Phosphate, PDB code: 1xbx
was solved by
E.L.Wise,
W.S.Yew,
J.Akana,
J.A.Gerlt,
I.Rayment,
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 Structure of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase E112D/R139V/T169A Mutant with Bound D-Ribulose 5-Phosphate
(pdb code 1xbx). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase E112D/R139V/T169A Mutant with Bound D-Ribulose 5-Phosphate, PDB code: 1xbx: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 1xbxGo back to Magnesium Binding Sites List in 1xbx
Magnesium binding site 1 out
of 2 in the Structure of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase E112D/R139V/T169A Mutant with Bound D-Ribulose 5-Phosphate
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 1xbxGo back to Magnesium Binding Sites List in 1xbx
Magnesium binding site 2 out
of 2 in the Structure of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase E112D/R139V/T169A Mutant with Bound D-Ribulose 5-Phosphate
Mono view Stereo pair view
Reference:
E.L.Wise,
W.S.Yew,
J.Akana,
J.A.Gerlt,
I.Rayment.
Evolution of Enzymatic Activities in the Orotidine 5'-Monophosphate Decarboxylase Suprafamily: Structural Basis For Catalytic Promiscuity in Wild-Type and Designed Mutants of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase Biochemistry V. 44 1816 2005.
Page generated: Tue Aug 13 17:29:35 2024
ISSN: ISSN 0006-2960 PubMed: 15697207 DOI: 10.1021/BI0478143 |
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