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Atomistry » Magnesium » PDB 5gre-5h1y » 5gtd » |
Magnesium in PDB 5gtd: O-Succinylbenzoate Coa Synthetase (Mene) From Bacillus Subtilis in Complex with the Acyl-Adenylate Intermediate Osb-AmpEnzymatic activity of O-Succinylbenzoate Coa Synthetase (Mene) From Bacillus Subtilis in Complex with the Acyl-Adenylate Intermediate Osb-Amp
All present enzymatic activity of O-Succinylbenzoate Coa Synthetase (Mene) From Bacillus Subtilis in Complex with the Acyl-Adenylate Intermediate Osb-Amp:
6.2.1.26; Protein crystallography data
The structure of O-Succinylbenzoate Coa Synthetase (Mene) From Bacillus Subtilis in Complex with the Acyl-Adenylate Intermediate Osb-Amp, PDB code: 5gtd
was solved by
Y.Chen,
Z.Guo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5gtd:
The structure of O-Succinylbenzoate Coa Synthetase (Mene) From Bacillus Subtilis in Complex with the Acyl-Adenylate Intermediate Osb-Amp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the O-Succinylbenzoate Coa Synthetase (Mene) From Bacillus Subtilis in Complex with the Acyl-Adenylate Intermediate Osb-Amp
(pdb code 5gtd). 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 O-Succinylbenzoate Coa Synthetase (Mene) From Bacillus Subtilis in Complex with the Acyl-Adenylate Intermediate Osb-Amp, PDB code: 5gtd: Magnesium binding site 1 out of 1 in 5gtdGo back to Magnesium Binding Sites List in 5gtd
Magnesium binding site 1 out
of 1 in the O-Succinylbenzoate Coa Synthetase (Mene) From Bacillus Subtilis in Complex with the Acyl-Adenylate Intermediate Osb-Amp
Mono view Stereo pair view
Reference:
Y.Chen,
Y.Jiang,
Z.Guo.
Mechanistic Insights From the Crystal Structure of Bacillus Subtilis O-Succinylbenzoyl-Coa Synthetase Complexed with the Adenylate Intermediate Biochemistry V. 55 6685 2016.
Page generated: Sun Sep 29 15:25:25 2024
ISSN: ISSN 1520-4995 PubMed: 27933791 DOI: 10.1021/ACS.BIOCHEM.6B00889 |
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