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Atomistry » Magnesium » PDB 6ftm-6g6y » 6fu2 » |
Magnesium in PDB 6fu2: Atp Phosphoribosyltransferase (Hiszg Atpprt) From Psychrobacter Arcticus in Complex with Prpp and AtpEnzymatic activity of Atp Phosphoribosyltransferase (Hiszg Atpprt) From Psychrobacter Arcticus in Complex with Prpp and Atp
All present enzymatic activity of Atp Phosphoribosyltransferase (Hiszg Atpprt) From Psychrobacter Arcticus in Complex with Prpp and Atp:
2.4.2.17; Protein crystallography data
The structure of Atp Phosphoribosyltransferase (Hiszg Atpprt) From Psychrobacter Arcticus in Complex with Prpp and Atp, PDB code: 6fu2
was solved by
M.S.Alphey,
Y.Ge,
G.Fisher,
C.M.Czekster,
J.H.Naismith,
R.G.Da Silva,
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 Atp Phosphoribosyltransferase (Hiszg Atpprt) From Psychrobacter Arcticus in Complex with Prpp and Atp
(pdb code 6fu2). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Atp Phosphoribosyltransferase (Hiszg Atpprt) From Psychrobacter Arcticus in Complex with Prpp and Atp, PDB code: 6fu2: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 6fu2Go back to Magnesium Binding Sites List in 6fu2
Magnesium binding site 1 out
of 2 in the Atp Phosphoribosyltransferase (Hiszg Atpprt) From Psychrobacter Arcticus in Complex with Prpp and Atp
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 6fu2Go back to Magnesium Binding Sites List in 6fu2
Magnesium binding site 2 out
of 2 in the Atp Phosphoribosyltransferase (Hiszg Atpprt) From Psychrobacter Arcticus in Complex with Prpp and Atp
Mono view Stereo pair view
Reference:
M.S.Alphey,
G.Fisher,
J.S.Hirschi,
R.Stroek,
Y.Ge,
E.R.Gould,
C.M.Czekster,
H.Liu,
G.J.Florence,
M.J.Vetticatt,
J.H.Naismith,
R.G.Da Silva.
Catalytic and Anticatalytic Snapshots of A Short-Form Atp Phosphoribosyltransferase Acs Catalysis 2018.
Page generated: Tue Oct 1 00:52:24 2024
ISSN: ESSN 2155-5435 DOI: 10.1021/ACSCATAL.8B00867 |
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