Zinc in PDB 4g4r: Mutm Containing F114A Mutation Bound to Oxog-Containing Dna

All present enzymatic activity of Mutm Containing F114A Mutation Bound to Oxog-Containing Dna:
3.2.2.23;

The structure of Mutm Containing F114A Mutation Bound to Oxog-Containing Dna, PDB code: 4g4r was solved by R.J.Sung, M.Zhang, Y.Qi, G.L.Verdine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.92 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.188, 93.541, 104.650, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 21.4

The binding sites of Zinc atom in the Mutm Containing F114A Mutation Bound to Oxog-Containing Dna (pdb code 4g4r). 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 Mutm Containing F114A Mutation Bound to Oxog-Containing Dna, PDB code: 4g4r:

Zinc binding site 1 out of 1 in the Mutm Containing F114A Mutation Bound to Oxog-Containing Dna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutm Containing F114A Mutation Bound to Oxog-Containing Dna within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:18.9 occ:1.00 SG A:CYS269 2.3 18.3 1.0 SG A:CYS249 2.3 16.7 1.0 SG A:CYS272 2.3 18.4 1.0 SG A:CYS252 2.3 18.3 1.0 CB A:CYS249 3.1 18.3 1.0 CB A:CYS272 3.3 15.9 1.0 CB A:CYS269 3.3 19.9 1.0 CB A:CYS252 3.4 15.5 1.0 N A:CYS272 3.7 15.7 1.0 N A:CYS252 3.9 17.0 1.0 CA A:CYS272 4.1 20.4 1.0 CE1 A:PHE182 4.1 17.0 1.0 CA A:CYS252 4.2 14.9 1.0 CB A:ARG271 4.5 16.2 1.0 CZ A:PHE182 4.6 19.7 1.0 CA A:CYS249 4.6 20.4 1.0 CB A:ARG251 4.6 18.1 1.0 CB A:THR254 4.7 25.2 1.0 C A:ARG251 4.7 19.7 1.0 C A:ARG271 4.7 17.3 1.0 CA A:CYS269 4.7 14.7 1.0 C A:CYS252 4.8 16.0 1.0 OG1 A:THR254 4.8 23.5 1.0 N A:GLY253 4.8 17.6 1.0 N A:THR254 5.0 19.9 1.0

R.J.Sung, M.Zhang, Y.Qi, G.L.Verdine. Structural and Biochemical Analysis of Dna Helix Invasion By the Bacterial 8-Oxoguanine Dna Glycosylase Mutm. J.Biol.Chem. V. 288 10012 2013.
ISSN: ISSN 0021-9258
PubMed: 23404556
DOI: 10.1074/JBC.M112.415612