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Atomistry » Magnesium » PDB 6akp-6asw » 6asm | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6akp-6asw » 6asm » |
Magnesium in PDB 6asm: E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to ThiosulfateEnzymatic activity of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate
All present enzymatic activity of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate:
4.1.1.49; Protein crystallography data
The structure of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate, PDB code: 6asm
was solved by
H.Y.H.Tang,
D.S.Shin,
J.A.Tainer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6asm:
The structure of E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate
(pdb code 6asm). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate, PDB code: 6asm: Magnesium binding site 1 out of 1 in 6asmGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the E. Coli Phosphoenolpyruvate Carboxykinase G209S K212C Mutant Bound to Thiosulfate
![]() Mono view ![]() Stereo pair view
Reference:
H.Y.H.Tang,
D.S.Shin,
G.L.Hura,
Y.Yang,
X.Hu,
F.C.Lightstone,
M.D.Mcgee,
H.S.Padgett,
S.M.Yannone,
J.A.Tainer.
Structural Control of Nonnative Ligand Binding in Engineered Mutants of Phosphoenolpyruvate Carboxykinase. Biochemistry V. 57 6688 2018.
Page generated: Mon Sep 30 19:20:55 2024
ISSN: ISSN 1520-4995 PubMed: 30376300 DOI: 10.1021/ACS.BIOCHEM.8B00963 |
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