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Zinc in PDB 2jg6: Crystal Structure of A 3-Methyladenine Dna Glycosylase I From Staphylococcus Aureus

Enzymatic activity of Crystal Structure of A 3-Methyladenine Dna Glycosylase I From Staphylococcus Aureus

All present enzymatic activity of Crystal Structure of A 3-Methyladenine Dna Glycosylase I From Staphylococcus Aureus:
3.2.2.20;

Protein crystallography data

The structure of Crystal Structure of A 3-Methyladenine Dna Glycosylase I From Staphylococcus Aureus, PDB code: 2jg6 was solved by X.Yan, L.G.Carter, H.Liu, M.Dorward, S.A.Mcmahon, K.A.Johnson, M.Oke, P.J.Coote, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.81 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 107.460, 63.098, 38.470, 90.00, 109.24, 90.00
R / Rfree (%) 16.3 / 19.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A 3-Methyladenine Dna Glycosylase I From Staphylococcus Aureus (pdb code 2jg6). 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 Crystal Structure of A 3-Methyladenine Dna Glycosylase I From Staphylococcus Aureus, PDB code: 2jg6:

Zinc binding site 1 out of 1 in 2jg6

Go back to Zinc Binding Sites List in 2jg6
Zinc binding site 1 out of 1 in the Crystal Structure of A 3-Methyladenine Dna Glycosylase I From Staphylococcus Aureus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A 3-Methyladenine Dna Glycosylase I From Staphylococcus Aureus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1187

b:18.5
occ:0.75
NE2 A:HIS17 2.1 18.5 1.0
ND1 A:HIS175 2.1 14.3 1.0
SG A:CYS179 2.3 17.8 1.0
SG A:CYS4 2.3 16.9 1.0
CE1 A:HIS17 2.7 20.0 1.0
CE1 A:HIS175 2.9 14.1 1.0
CB A:CYS4 3.2 18.6 1.0
CB A:CYS179 3.2 19.1 1.0
CG A:HIS175 3.2 14.0 1.0
CD2 A:HIS17 3.3 19.3 1.0
CB A:HIS175 3.7 14.2 1.0
ND1 A:HIS17 3.9 19.3 1.0
CA A:HIS175 4.1 14.2 1.0
NE2 A:HIS175 4.1 14.5 1.0
CG A:HIS17 4.2 17.5 1.0
CD2 A:HIS175 4.3 14.2 1.0
CB A:SER181 4.4 16.4 1.0
CA A:CYS4 4.5 18.7 1.0
N A:LEU176 4.5 15.1 1.0
C A:CYS4 4.6 19.2 1.0
CZ3 A:TRP21 4.6 16.6 1.0
CA A:CYS179 4.7 19.2 1.0
C A:HIS175 4.8 14.7 1.0
O A:CYS4 4.9 19.1 1.0
CE3 A:TRP21 4.9 15.5 1.0
N A:ALA5 5.0 20.1 1.0
N A:SER181 5.0 16.8 1.0
C A:SER181 5.0 15.2 1.0

Reference:

M.Oke, L.G.Carter, K.A.Johnson, H.Liu, S.A.Mcmahon, X.Yan, M.Kerou, N.D.Weikart, N.Kadi, M.A.Sheikh, S.Schmelz, M.Dorward, M.Zawadzki, C.Cozens, H.Falconer, H.Powers, I.M.Overton, C.A.J.Van Niekerk, X.Peng, P.Patel, R.A.Garrett, D.Prangishvili, C.H.Botting, P.J.Coote, D.T.F.Dryden, G.J.Barton, U.Schwarz-Linek, G.L.Challis, G.L.Taylor, M.F.White, J.H.Naismith. The Scottish Structural Proteomics Facility: Targets, Methods and Outputs. J.Struct.Funct.Genomics V. 11 167 2010.
ISSN: ISSN 1345-711X
PubMed: 20419351
DOI: 10.1007/S10969-010-9090-Y
Page generated: Wed Dec 16 03:32:01 2020

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