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Atomistry » Caesium » PDB 1av2-2j9x » 1uzm | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Caesium » PDB 1av2-2j9x » 1uzm » |
Caesium in PDB 1uzm: Maba From Mycobacterium TuberculosisEnzymatic activity of Maba From Mycobacterium Tuberculosis
All present enzymatic activity of Maba From Mycobacterium Tuberculosis:
1.1.1.100; Protein crystallography data
The structure of Maba From Mycobacterium Tuberculosis, PDB code: 1uzm
was solved by
M.Cohen-Gonsaud,
S.Ducasse,
A.Quemard,
G.Labesse,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Caesium Binding Sites:
The binding sites of Caesium atom in the Maba From Mycobacterium Tuberculosis
(pdb code 1uzm). This binding sites where shown within
5.0 Angstroms radius around Caesium atom.
In total 4 binding sites of Caesium where determined in the Maba From Mycobacterium Tuberculosis, PDB code: 1uzm: Jump to Caesium binding site number: 1; 2; 3; 4; Caesium binding site 1 out of 4 in 1uzmGo back to Caesium Binding Sites List in 1uzm
Caesium binding site 1 out
of 4 in the Maba From Mycobacterium Tuberculosis
Mono view Stereo pair view
Caesium binding site 2 out of 4 in 1uzmGo back to Caesium Binding Sites List in 1uzm
Caesium binding site 2 out
of 4 in the Maba From Mycobacterium Tuberculosis
Mono view Stereo pair view
Caesium binding site 3 out of 4 in 1uzmGo back to Caesium Binding Sites List in 1uzm
Caesium binding site 3 out
of 4 in the Maba From Mycobacterium Tuberculosis
Mono view Stereo pair view
Caesium binding site 4 out of 4 in 1uzmGo back to Caesium Binding Sites List in 1uzm
Caesium binding site 4 out
of 4 in the Maba From Mycobacterium Tuberculosis
Mono view Stereo pair view
Reference:
M.Cohen-Gonsaud,
S.Ducasse,
F.Hoh,
D.Zerbib,
G.Labesse,
A.Quemard.
Crystal Structure of Maba From Mycobacterium Tuberculosis, A Reductase Involved in Long-Chain Fatty Acid Biosynthesis. J.Mol.Biol. V. 320 249 2002.
Page generated: Tue Jul 30 20:15:51 2024
ISSN: ISSN 0022-2836 PubMed: 12079383 DOI: 10.1016/S0022-2836(02)00463-1 |
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