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Atomistry » Magnesium » PDB 5v60-5voi » 5vg7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 5v60-5voi » 5vg7 » |
Magnesium in PDB 5vg7: Crystal Structure of the R503Q Missense Variant of Human PGM1Enzymatic activity of Crystal Structure of the R503Q Missense Variant of Human PGM1
All present enzymatic activity of Crystal Structure of the R503Q Missense Variant of Human PGM1:
5.4.2.2; Protein crystallography data
The structure of Crystal Structure of the R503Q Missense Variant of Human PGM1, PDB code: 5vg7
was solved by
K.M.Stiers,
L.J.Beamer,
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 Crystal Structure of the R503Q Missense Variant of Human PGM1
(pdb code 5vg7). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the R503Q Missense Variant of Human PGM1, PDB code: 5vg7: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 5vg7Go back to Magnesium Binding Sites List in 5vg7
Magnesium binding site 1 out
of 2 in the Crystal Structure of the R503Q Missense Variant of Human PGM1
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 5vg7Go back to Magnesium Binding Sites List in 5vg7
Magnesium binding site 2 out
of 2 in the Crystal Structure of the R503Q Missense Variant of Human PGM1
Mono view Stereo pair view
Reference:
K.M.Stiers,
L.J.Beamer.
A Hotspot For Disease-Associated Variants of Human PGM1 Is Associated with Impaired Ligand Binding and Loop Dynamics. Structure V. 26 1337 2018.
Page generated: Mon Sep 30 06:10:25 2024
ISSN: ISSN 1878-4186 PubMed: 30122451 DOI: 10.1016/J.STR.2018.07.005 |
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