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Atomistry » Zinc » PDB 3lt8-3m1j » 3lt8 » |
Zinc in PDB 3lt8: A Non-Biological Atp Binding Protein with A Single Point Mutation (D65V), That Contributes to Optimized Folding and Ligand Binding, Crystallized in the Presence of 100 Mm Atp.Protein crystallography data
The structure of A Non-Biological Atp Binding Protein with A Single Point Mutation (D65V), That Contributes to Optimized Folding and Ligand Binding, Crystallized in the Presence of 100 Mm Atp., PDB code: 3lt8
was solved by
C.R.Simmons,
C.L.Magee,
J.P.Allen,
J.C.Chaput,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3lt8:
The structure of A Non-Biological Atp Binding Protein with A Single Point Mutation (D65V), That Contributes to Optimized Folding and Ligand Binding, Crystallized in the Presence of 100 Mm Atp. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the A Non-Biological Atp Binding Protein with A Single Point Mutation (D65V), That Contributes to Optimized Folding and Ligand Binding, Crystallized in the Presence of 100 Mm Atp.
(pdb code 3lt8). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the A Non-Biological Atp Binding Protein with A Single Point Mutation (D65V), That Contributes to Optimized Folding and Ligand Binding, Crystallized in the Presence of 100 Mm Atp., PDB code: 3lt8: Zinc binding site 1 out of 1 in 3lt8Go back to Zinc Binding Sites List in 3lt8
Zinc binding site 1 out
of 1 in the A Non-Biological Atp Binding Protein with A Single Point Mutation (D65V), That Contributes to Optimized Folding and Ligand Binding, Crystallized in the Presence of 100 Mm Atp.
Mono view Stereo pair view
Reference:
C.R.Simmons,
C.L.Magee,
D.A.Smith,
L.Lauman,
J.C.Chaput,
J.P.Allen.
Three-Dimensional Structures Reveal Multiple Adp/Atp Binding Modes For A Synthetic Class of Artificial Proteins. Biochemistry V. 49 8689 2010.
Page generated: Wed Dec 16 04:33:03 2020
ISSN: ISSN 0006-2960 PubMed: 20822107 DOI: 10.1021/BI100398P |
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