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Zinc in PDB 3lt9: A Non-Biological Atp Binding Protein with A Single Point Mutation (D65V), That Contributes to Optimized Folding and Ligand Binding

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, PDB code: 3lt9 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

Other elements in 3lt9:

The structure of A Non-Biological Atp Binding Protein with A Single Point Mutation (D65V), That Contributes to Optimized Folding and Ligand Binding also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

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 (pdb code 3lt9). 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, PDB code: 3lt9:

Zinc binding site 1 out of 1 in 3lt9

Go back to Zinc Binding Sites List in 3lt9
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


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 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

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.
ISSN: ISSN 0006-2960
PubMed: 20822107
DOI: 10.1021/BI100398P
Page generated: Wed Dec 16 04:33:03 2020

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