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Magnesium in PDB 7kb1: Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction IntermediateProtein crystallography data
The structure of Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate, PDB code: 7kb1
was solved by
J.L.Brewster,
P.Pachl,
C.Squire,
M.Selmer,
W.M.Patrick,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7kb1:
The structure of Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate
(pdb code 7kb1). 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 Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate, PDB code: 7kb1: Magnesium binding site 1 out of 1 in 7kb1Go back to Magnesium Binding Sites List in 7kb1
Magnesium binding site 1 out
of 1 in the Complex of O-Acety-L-Homoserine Aminocarboxypropyltransferase (Mety) From Thermotoga Maritima and A Key Reaction Intermediate
Mono view Stereo pair view
Reference:
J.L.Brewster,
P.Pachl,
J.L.O.Mckellar,
M.Selmer,
C.J.Squire,
W.M.Patrick.
Structures and Kinetics of Thermotoga Maritima Mety Reveal New Insights Into the Predominant Sulfurylation Enzyme of Bacterial Methionine Biosynthesis. J.Biol.Chem. 00797 2021.
Page generated: Sun Jul 11 17:41:42 2021
ISSN: ESSN 1083-351X PubMed: 34019879 DOI: 10.1016/J.JBC.2021.100797 |
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