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Atomistry » Cobalt » PDB 1a0c-1e1c » 1cia » |
Cobalt in PDB 1cia: Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For GlutamateEnzymatic activity of Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For Glutamate
All present enzymatic activity of Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For Glutamate:
2.3.1.28; Protein crystallography data
The structure of Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For Glutamate, PDB code: 1cia
was solved by
A.G.W.Leslie,
M.R.Gibbs,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For Glutamate
(pdb code 1cia). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For Glutamate, PDB code: 1cia: Jump to Cobalt binding site number: 1; 2; Cobalt binding site 1 out of 2 in 1ciaGo back to![]() ![]()
Cobalt binding site 1 out
of 2 in the Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For Glutamate
![]() Mono view ![]() Stereo pair view
Cobalt binding site 2 out of 2 in 1ciaGo back to![]() ![]()
Cobalt binding site 2 out
of 2 in the Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For Glutamate
![]() Mono view ![]() Stereo pair view
Reference:
A.Lewendon,
I.A.Murray,
W.V.Shaw,
M.R.Gibbs,
A.G.Leslie.
Replacement of Catalytic Histidine-195 of Chloramphenicol Acetyltransferase: Evidence For A General Base Role For Glutamate. Biochemistry V. 33 1944 1994.
Page generated: Sun Jul 13 17:25:41 2025
ISSN: ISSN 0006-2960 PubMed: 7906544 DOI: 10.1021/BI00173A043 |
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