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Atomistry » Cobalt » PDB 3bbk-3ger » 3dj4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cobalt » PDB 3bbk-3ger » 3dj4 » |
Cobalt in PDB 3dj4: Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.Enzymatic activity of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.
All present enzymatic activity of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.:
2.3.1.157; 2.7.7.23; Protein crystallography data
The structure of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine., PDB code: 3dj4
was solved by
S.K.Verma,
B.Prakash,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3dj4:
The structure of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine. also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.
(pdb code 3dj4). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine., PDB code: 3dj4: Cobalt binding site 1 out of 1 in 3dj4Go back to Cobalt Binding Sites List in 3dj4
Cobalt binding site 1 out
of 1 in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.
Mono view Stereo pair view
Reference:
A.Parikh,
S.K.Verma,
S.Khan,
B.Prakash,
V.K.Nandicoori.
Pknb-Mediated Phosphorylation of A Novel Substrate, N-Acetylglucosamine-1-Phosphate Uridyltransferase, Modulates Its Acetyltransferase Activity. J.Mol.Biol. V. 386 451 2009.
Page generated: Tue Jul 30 15:52:59 2024
ISSN: ISSN 0022-2836 PubMed: 19121323 DOI: 10.1016/J.JMB.2008.12.031 |
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