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Atomistry » Cobalt » PDB 1nyi-1rr2 » 1r6x » |
Cobalt in PDB 1r6x: The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with SulfateEnzymatic activity of The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate
All present enzymatic activity of The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate:
2.7.7.4; Protein crystallography data
The structure of The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate, PDB code: 1r6x
was solved by
D.J.Lalor,
T.Schnyder,
V.Saridakis,
D.E.Pilloff,
A.Dong,
H.Tang,
T.S.Leyh,
E.F.Pai,
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 Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate
(pdb code 1r6x). 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 Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate, PDB code: 1r6x: Cobalt binding site 1 out of 1 in 1r6xGo back to Cobalt Binding Sites List in 1r6x
Cobalt binding site 1 out
of 1 in the The Crystal Structure of A Truncated Form of Yeast Atp Sulfurylase, Lacking the C-Terminal Aps Kinase-Like Domain, in Complex with Sulfate
Mono view Stereo pair view
Reference:
D.J.Lalor,
T.Schnyder,
V.Saridakis,
D.E.Pilloff,
A.Dong,
H.Tang,
T.S.Leyh,
E.F.Pai.
Structural and Functional Analysis of A Truncated Form of Saccharomyces Cerevisiae Atp Sulfurylase: C-Terminal Domain Essential For Oligomer Formation But Not For Activity Protein Eng. V. 16 1071 2003.
Page generated: Tue Jul 30 14:33:57 2024
ISSN: ISSN 0269-2139 PubMed: 14983089 DOI: 10.1093/PROTEIN/GZG133 |
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