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Atomistry » Chlorine » PDB 5cai-5cmt » 5cgm » |
Chlorine in PDB 5cgm: Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A ResolutionEnzymatic activity of Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A Resolution
All present enzymatic activity of Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A Resolution:
2.4.99.16; Protein crystallography data
The structure of Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A Resolution, PDB code: 5cgm
was solved by
V.Mendes,
M.Blaszczyk,
A.Maranha,
N.Empadinhas,
T.L.Blundell,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5cgm:
The structure of Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A Resolution also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A Resolution
(pdb code 5cgm). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A Resolution, PDB code: 5cgm: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 5cgmGo back to Chlorine Binding Sites List in 5cgm
Chlorine binding site 1 out
of 2 in the Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A Resolution
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 5cgmGo back to Chlorine Binding Sites List in 5cgm
Chlorine binding site 2 out
of 2 in the Structure of Mycobacterium Thermoresistibile Glge in Complex with Maltose at 1.95A Resolution
Mono view Stereo pair view
Reference:
V.Mendes,
M.Blaszczyk,
A.Maranha,
N.Empadinhas,
T.L.Blundell.
Structure of Mycobacterium Thermoresistibile Glge Defines Novel Conformational States That Contribute to the Catalytic Mechanism. Sci Rep V. 5 17144 2015.
Page generated: Sat Dec 12 11:35:11 2020
ISSN: ESSN 2045-2322 PubMed: 26616850 DOI: 10.1038/SREP17144 |
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