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Atomistry » Tungsten » PDB 4z3x-6rvg » 5c66 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Tungsten » PDB 4z3x-6rvg » 5c66 » |
Tungsten in PDB 5c66: E. Coli Alkaline Phosphatase in Complex with TungstateEnzymatic activity of E. Coli Alkaline Phosphatase in Complex with Tungstate
All present enzymatic activity of E. Coli Alkaline Phosphatase in Complex with Tungstate:
3.1.3.1; Protein crystallography data
The structure of E. Coli Alkaline Phosphatase in Complex with Tungstate, PDB code: 5c66
was solved by
A.Peck,
D.Herschlag,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5c66:
The structure of E. Coli Alkaline Phosphatase in Complex with Tungstate also contains other interesting chemical elements:
Tungsten Binding Sites:
The binding sites of Tungsten atom in the E. Coli Alkaline Phosphatase in Complex with Tungstate
(pdb code 5c66). This binding sites where shown within
5.0 Angstroms radius around Tungsten atom.
In total 2 binding sites of Tungsten where determined in the E. Coli Alkaline Phosphatase in Complex with Tungstate, PDB code: 5c66: Jump to Tungsten binding site number: 1; 2; Tungsten binding site 1 out of 2 in 5c66Go back to Tungsten Binding Sites List in 5c66
Tungsten binding site 1 out
of 2 in the E. Coli Alkaline Phosphatase in Complex with Tungstate
Mono view Stereo pair view
Tungsten binding site 2 out of 2 in 5c66Go back to Tungsten Binding Sites List in 5c66
Tungsten binding site 2 out
of 2 in the E. Coli Alkaline Phosphatase in Complex with Tungstate
Mono view Stereo pair view
Reference:
A.Peck,
F.Sunden,
L.D.Andrews,
V.S.Pande,
D.Herschlag.
Tungstate As A Transition State Analog For Catalysis By Alkaline Phosphatase. J.Mol.Biol. V. 428 2758 2016.
Page generated: Wed Dec 16 02:35:02 2020
ISSN: ESSN 1089-8638 PubMed: 27189921 DOI: 10.1016/J.JMB.2016.05.007 |
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