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.

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:

Resolution Low / High (Å)	41.34 / 2.55
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.461, 71.461, 55.583, 90.00, 90.00, 120.00
R / Rfree (%)	17.8 / 23.9

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:

Chlorine

(Cl)

1 atom

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 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

A full contact list of Zinc with other atoms in the Zn binding site number 1 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. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn80 b:37.8 occ:1.00 SG A:CYS26 2.3 35.7 1.0 SG A:CYS23 2.3 29.3 1.0 SG A:CYS49 2.4 30.5 1.0 SG A:CYS46 2.5 27.8 1.0 CB A:CYS23 3.1 29.8 1.0 CB A:CYS26 3.1 34.6 1.0 CB A:CYS49 3.2 28.7 1.0 N A:CYS26 3.6 33.9 1.0 CB A:CYS46 3.8 27.5 1.0 CA A:CYS26 3.9 34.8 1.0 N A:CYS46 4.0 27.1 1.0 CB A:ALA29 4.3 32.0 1.0 N A:CYS49 4.4 28.4 1.0 CA A:CYS49 4.4 28.7 1.0 CA A:CYS46 4.5 27.7 1.0 CA A:CYS23 4.6 30.3 1.0 C A:LYS25 4.7 33.1 1.0 C A:CYS26 4.7 35.2 1.0 CB A:LYS25 4.8 31.8 1.0 N A:LYS27 4.8 35.8 1.0 N A:LYS25 5.0 32.4 1.0

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.
ISSN: ISSN 0006-2960
PubMed: 20822107
DOI: 10.1021/BI100398P