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Magnesium in PDB 6et9: Structure of the Acetoacetyl-Coa-Thiolase/Hmg-Coa-Synthase Complex From Methanothermococcus Thermolithotrophicus at 2.75 AEnzymatic activity of Structure of the Acetoacetyl-Coa-Thiolase/Hmg-Coa-Synthase Complex From Methanothermococcus Thermolithotrophicus at 2.75 A
All present enzymatic activity of Structure of the Acetoacetyl-Coa-Thiolase/Hmg-Coa-Synthase Complex From Methanothermococcus Thermolithotrophicus at 2.75 A:
2.3.1.9; 2.3.3.10; Protein crystallography data
The structure of Structure of the Acetoacetyl-Coa-Thiolase/Hmg-Coa-Synthase Complex From Methanothermococcus Thermolithotrophicus at 2.75 A, PDB code: 6et9
was solved by
S.Engilberge,
B.Voegeli,
E.Girard,
F.Riobe,
O.Maury,
T.J.Erb,
S.Shima,
T.Wagner,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6et9:
The structure of Structure of the Acetoacetyl-Coa-Thiolase/Hmg-Coa-Synthase Complex From Methanothermococcus Thermolithotrophicus at 2.75 A also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of the Acetoacetyl-Coa-Thiolase/Hmg-Coa-Synthase Complex From Methanothermococcus Thermolithotrophicus at 2.75 A
(pdb code 6et9). 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 Structure of the Acetoacetyl-Coa-Thiolase/Hmg-Coa-Synthase Complex From Methanothermococcus Thermolithotrophicus at 2.75 A, PDB code: 6et9: Magnesium binding site 1 out of 1 in 6et9Go back to Magnesium Binding Sites List in 6et9
Magnesium binding site 1 out
of 1 in the Structure of the Acetoacetyl-Coa-Thiolase/Hmg-Coa-Synthase Complex From Methanothermococcus Thermolithotrophicus at 2.75 A
Mono view Stereo pair view
Reference:
B.Vogeli,
S.Engilberge,
E.Girard,
F.Riobe,
O.Maury,
T.J.Erb,
S.Shima,
T.Wagner.
Archaeal Acetoacetyl-Coa Thiolase/Hmg-Coa Synthase Complex Channels the Intermediate Via A Fused Coa-Binding Site. Proc. Natl. Acad. Sci. V. 115 3380 2018U.S.A..
Page generated: Mon Dec 14 22:39:20 2020
ISSN: ESSN 1091-6490 PubMed: 29531083 DOI: 10.1073/PNAS.1718649115 |
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