Zinc in PDB 3jr5: Mutm Lesion Recognition Control Complex with N174C Crosslinking Site

All present enzymatic activity of Mutm Lesion Recognition Control Complex with N174C Crosslinking Site:
4.2.99.18;

The structure of Mutm Lesion Recognition Control Complex with N174C Crosslinking Site, PDB code: 3jr5 was solved by Y.Qi, M.C.Spong, G.L.Verdine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.03 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.343, 95.377, 102.482, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 18.5

The binding sites of Zinc atom in the Mutm Lesion Recognition Control Complex with N174C Crosslinking Site (pdb code 3jr5). 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 Lesion Recognition Control Complex with N174C Crosslinking Site, PDB code: 3jr5:

Zinc binding site 1 out of 1 in the Mutm Lesion Recognition Control Complex with N174C Crosslinking Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutm Lesion Recognition Control Complex with N174C Crosslinking Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:19.3 occ:1.00 SG A:CYS272 2.3 17.0 1.0 SG A:CYS252 2.3 13.8 1.0 SG A:CYS249 2.4 13.2 1.0 SG A:CYS269 2.4 13.6 1.0 CB A:CYS249 3.2 11.7 1.0 CB A:CYS272 3.4 14.0 1.0 CB A:CYS252 3.4 17.2 1.0 CB A:CYS269 3.4 10.9 1.0 N A:CYS272 3.8 14.4 1.0 N A:CYS252 3.9 14.4 1.0 CE1 A:PHE182 4.1 12.5 1.0 CA A:CYS272 4.2 11.7 1.0 CA A:CYS252 4.2 12.7 1.0 CB A:ARG271 4.6 15.4 1.0 CZ A:PHE182 4.6 14.3 1.0 CA A:CYS249 4.6 15.0 1.0 CB A:ARG251 4.7 17.0 1.0 C A:ARG251 4.8 18.8 1.0 C A:ARG271 4.8 16.4 1.0 CA A:CYS269 4.8 13.7 1.0 CB A:THR254 4.8 15.8 1.0 C A:CYS252 4.9 13.8 1.0 N A:GLY253 4.9 14.8 1.0 OG1 A:THR254 5.0 16.6 1.0

Y.Qi, M.C.Spong, K.Nam, M.Karplus, G.L.Verdine. Entrapment and Structure of An Extrahelical Guanine Attempting to Enter the Active Site of A Bacterial Dna Glycosylase, Mutm. J.Biol.Chem. V. 285 1468 2010.
ISSN: ISSN 0021-9258
PubMed: 19889642
DOI: 10.1074/JBC.M109.069799