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Atomistry » Bromine » PDB 4z91-5c9w » 5c9w » |
Bromine in PDB 5c9w: Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with (Z)-N-(2-Bromophenyl)-2-(Hydroxyimino)AcetamideEnzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with (Z)-N-(2-Bromophenyl)-2-(Hydroxyimino)Acetamide
All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with (Z)-N-(2-Bromophenyl)-2-(Hydroxyimino)Acetamide:
2.3.3.9; Protein crystallography data
The structure of Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with (Z)-N-(2-Bromophenyl)-2-(Hydroxyimino)Acetamide, PDB code: 5c9w
was solved by
H.-L.Huang,
J.C.Sacchettini,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5c9w:
The structure of Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with (Z)-N-(2-Bromophenyl)-2-(Hydroxyimino)Acetamide also contains other interesting chemical elements:
Bromine Binding Sites:
The binding sites of Bromine atom in the Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with (Z)-N-(2-Bromophenyl)-2-(Hydroxyimino)Acetamide
(pdb code 5c9w). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with (Z)-N-(2-Bromophenyl)-2-(Hydroxyimino)Acetamide, PDB code: 5c9w: Bromine binding site 1 out of 1 in 5c9wGo back to Bromine Binding Sites List in 5c9w
Bromine binding site 1 out
of 1 in the Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with (Z)-N-(2-Bromophenyl)-2-(Hydroxyimino)Acetamide
Mono view Stereo pair view
Reference:
H.L.Huang,
I.V.Krieger,
M.K.Parai,
V.B.Gawandi,
J.C.Sacchettini.
Mycobacterium Tuberculosis Malate Synthase Structures with Fragments Reveal A Portal For Substrate/Product Exchange. J. Biol. Chem. V. 291 27421 2016.
Page generated: Wed Jul 10 23:22:01 2024
ISSN: ESSN 1083-351X PubMed: 27738104 DOI: 10.1074/JBC.M116.750877 |
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