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Atomistry » Zinc » PDB 1uio-1uzf » 1uwz | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1uio-1uzf » 1uwz » |
Zinc in PDB 1uwz: Bacillus Subtilis Cytidine Deaminase with An ARG56 - Ala SubstitutionEnzymatic activity of Bacillus Subtilis Cytidine Deaminase with An ARG56 - Ala Substitution
All present enzymatic activity of Bacillus Subtilis Cytidine Deaminase with An ARG56 - Ala Substitution:
3.5.4.5; Protein crystallography data
The structure of Bacillus Subtilis Cytidine Deaminase with An ARG56 - Ala Substitution, PDB code: 1uwz
was solved by
E.Johansson,
J.Neuhard,
M.Willemoes,
S.Larsen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Bacillus Subtilis Cytidine Deaminase with An ARG56 - Ala Substitution
(pdb code 1uwz). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Bacillus Subtilis Cytidine Deaminase with An ARG56 - Ala Substitution, PDB code: 1uwz: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1uwzGo back to Zinc Binding Sites List in 1uwz
Zinc binding site 1 out
of 2 in the Bacillus Subtilis Cytidine Deaminase with An ARG56 - Ala Substitution
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1uwzGo back to Zinc Binding Sites List in 1uwz
Zinc binding site 2 out
of 2 in the Bacillus Subtilis Cytidine Deaminase with An ARG56 - Ala Substitution
Mono view Stereo pair view
Reference:
E.Johansson,
J.Neuhard,
M.Willemoes,
S.Larsen.
Structural, Kinetic, and Mutational Studies of the Zinc Ion Environment in Tetrameric Cytidine Deaminase Biochemistry V. 43 6020 2004.
Page generated: Wed Oct 16 19:38:56 2024
ISSN: ISSN 0006-2960 PubMed: 15147186 DOI: 10.1021/BI035893X |
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