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Atomistry » Potassium » PDB 3ccm-3dke » 3den | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 3ccm-3dke » 3den » |
Potassium in PDB 3den: Structure of E. Coli Dhdps Mutant Y107WEnzymatic activity of Structure of E. Coli Dhdps Mutant Y107W
All present enzymatic activity of Structure of E. Coli Dhdps Mutant Y107W:
4.2.1.52; Protein crystallography data
The structure of Structure of E. Coli Dhdps Mutant Y107W, PDB code: 3den
was solved by
F.G.Pearce,
J.A.Gerrard,
M.A.Perugini,
G.B.Jameson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of E. Coli Dhdps Mutant Y107W
(pdb code 3den). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of E. Coli Dhdps Mutant Y107W, PDB code: 3den: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 3denGo back to Potassium Binding Sites List in 3den
Potassium binding site 1 out
of 2 in the Structure of E. Coli Dhdps Mutant Y107W
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 3denGo back to Potassium Binding Sites List in 3den
Potassium binding site 2 out
of 2 in the Structure of E. Coli Dhdps Mutant Y107W
Mono view Stereo pair view
Reference:
F.G.Pearce,
R.C.J.Dobson,
A.Weber,
L.A.Lane,
M.G.Mccammon,
M.A.Squire,
M.A.Perugini,
G.B.Jameson,
C.V.Robinson,
J.A.Gerrard.
Mutating the Tight-Dimer Interface of Dihydrodipicolinate Synthase Disrupts the Enzyme Quaternary Structure: Toward A Monomeric Enzyme Biochemistry V. 47 12108 2008.
Page generated: Sun Dec 13 23:17:30 2020
ISSN: ISSN 0006-2960 PubMed: 18937497 DOI: 10.1021/BI801094T |
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