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Atomistry » Cobalt » PDB 1zfv-2dfi » 2c79 » |
Cobalt in PDB 2c79: The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.Enzymatic activity of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.
All present enzymatic activity of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.:
3.1.1.72; Protein crystallography data
The structure of The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion., PDB code: 2c79
was solved by
E.J.Taylor,
P.J.Turkenburg,
F.Vincent,
A.M.Brzozowski,
T.M.Gloster,
C.Dupont,
F.Shareck,
M.S.J.Centeno,
J.A.M.Prates,
L.M.A.Ferreira,
C.M.G.A.Fontes,
P.Biely,
G.J.Davies,
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 The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.
(pdb code 2c79). 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 The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion., PDB code: 2c79: Cobalt binding site 1 out of 1 in 2c79Go back to Cobalt Binding Sites List in 2c79
Cobalt binding site 1 out
of 1 in the The Structure of A Family 4 Acetyl Xylan Esterase From Clostridium Thermocellum in Complex with A Colbalt Ion.
Mono view Stereo pair view
Reference:
E.J.Taylor,
T.M.Gloster,
P.J.Turkenburg,
F.Vincent,
A.M.Brzozowski,
C.Dupont,
F.Shareck,
M.S.J.Centeno,
J.A.M.Prates,
V.Puchart,
L.M.A.Ferreira,
C.M.G.A.Fontes,
P.Biely,
G.J.Davies.
Structure and Activity of Two Metal-Ion Dependent Acetyl Xylan Esterases Involved in Plant Cell Wall Degradation Reveals A Close Similarity to Peptidoglycan Deacetylases. J.Biol.Chem. V. 281 10968 2006.
Page generated: Sun Dec 13 10:37:16 2020
ISSN: ISSN 0021-9258 PubMed: 16431911 DOI: 10.1074/JBC.M513066200 |
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