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Atomistry » Manganese » PDB 6a9v-6bh4 » 6at2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 6a9v-6bh4 » 6at2 » |
Manganese in PDB 6at2: E. Coli Phosphoenolpyruvate Carboxykinase G209N Mutant Bound to ThiosulfateEnzymatic activity of E. Coli Phosphoenolpyruvate Carboxykinase G209N Mutant Bound to Thiosulfate
All present enzymatic activity of E. Coli Phosphoenolpyruvate Carboxykinase G209N Mutant Bound to Thiosulfate:
4.1.1.49; Protein crystallography data
The structure of E. Coli Phosphoenolpyruvate Carboxykinase G209N Mutant Bound to Thiosulfate, PDB code: 6at2
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 6at2:
The structure of E. Coli Phosphoenolpyruvate Carboxykinase G209N Mutant Bound to Thiosulfate also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the E. Coli Phosphoenolpyruvate Carboxykinase G209N Mutant Bound to Thiosulfate
(pdb code 6at2). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the E. Coli Phosphoenolpyruvate Carboxykinase G209N Mutant Bound to Thiosulfate, PDB code: 6at2: Manganese binding site 1 out of 1 in 6at2Go back to Manganese Binding Sites List in 6at2
Manganese binding site 1 out
of 1 in the E. Coli Phosphoenolpyruvate Carboxykinase G209N 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: Tue Dec 15 04:50:43 2020
ISSN: ISSN 1520-4995 PubMed: 30376300 DOI: 10.1021/ACS.BIOCHEM.8B00963 |
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