Zinc in PDB 3u6m: Structural Effects of Sequence Context on Lesion Recognition By Mutm

All present enzymatic activity of Structural Effects of Sequence Context on Lesion Recognition By Mutm:
3.2.2.23;

The structure of Structural Effects of Sequence Context on Lesion Recognition By Mutm, PDB code: 3u6m 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)	32.69 / 2.10
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 (%)	18.8 / 22.4

The binding sites of Zinc atom in the Structural Effects of Sequence Context on Lesion Recognition By Mutm (pdb code 3u6m). 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 Structural Effects of Sequence Context on Lesion Recognition By Mutm, PDB code: 3u6m:

Zinc binding site 1 out of 1 in the Structural Effects of Sequence Context on Lesion Recognition By Mutm


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Effects of Sequence Context on Lesion Recognition By Mutm within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:24.7 occ:1.00 SG A:CYS272 2.3 22.4 1.0 SG A:CYS269 2.3 23.8 1.0 SG A:CYS249 2.4 23.3 1.0 SG A:CYS252 2.4 20.9 1.0 CB A:CYS249 3.1 25.5 1.0 CB A:CYS269 3.3 20.9 1.0 CB A:CYS272 3.3 16.4 1.0 CB A:CYS252 3.4 25.6 1.0 N A:CYS272 3.7 24.4 1.0 N A:CYS252 3.9 25.9 1.0 CA A:CYS272 4.1 22.6 1.0 CE1 A:PHE182 4.1 23.9 1.0 CA A:CYS252 4.2 23.5 1.0 CB A:ARG251 4.4 28.3 0.5 CB A:ARG271 4.6 25.9 1.0 CA A:CYS249 4.6 24.8 1.0 CZ A:PHE182 4.7 26.3 1.0 C A:ARG251 4.7 25.6 0.5 CA A:CYS269 4.7 23.0 1.0 C A:ARG271 4.8 25.7 1.0 CB A:ARG251 4.8 26.9 0.5 C A:ARG251 4.8 25.7 0.5 C A:CYS252 4.8 24.1 1.0 CB A:THR254 4.8 27.6 1.0 N A:GLY253 4.9 24.6 1.0

R.J.Sung, M.Zhang, Y.Qi, G.L.Verdine. Sequence-Dependent Structural Variation in Dna Undergoing Intrahelical Inspection By the Dna Glycosylase Mutm. J.Biol.Chem. V. 287 18044 2012.
ISSN: ISSN 0021-9258
PubMed: 22465958
DOI: 10.1074/JBC.M111.313635