Zinc in PDB 2f5q: Catalytically Inactive (E3Q) Mutm Crosslinked to Oxog:C Containing Dna CC2

All present enzymatic activity of Catalytically Inactive (E3Q) Mutm Crosslinked to Oxog:C Containing Dna CC2:
3.2.2.23;

The structure of Catalytically Inactive (E3Q) Mutm Crosslinked to Oxog:C Containing Dna CC2, PDB code: 2f5q was solved by A.Banerjee, W.L.Santos, G.L.Verdine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.00 / 2.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.413, 92.000, 103.050, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 24.9

The binding sites of Zinc atom in the Catalytically Inactive (E3Q) Mutm Crosslinked to Oxog:C Containing Dna CC2 (pdb code 2f5q). 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 Catalytically Inactive (E3Q) Mutm Crosslinked to Oxog:C Containing Dna CC2, PDB code: 2f5q:

Zinc binding site 1 out of 1 in the Catalytically Inactive (E3Q) Mutm Crosslinked to Oxog:C Containing Dna CC2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Catalytically Inactive (E3Q) Mutm Crosslinked to Oxog:C Containing Dna CC2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:35.8 occ:1.00 SG A:CYS249 2.4 36.0 1.0 SG A:CYS269 2.4 37.0 1.0 SG A:CYS252 2.5 37.4 1.0 SG A:CYS272 2.7 40.4 1.0 CB A:CYS249 3.2 38.0 1.0 CB A:CYS269 3.4 37.7 1.0 CB A:CYS252 3.4 36.9 1.0 CB A:CYS272 3.5 40.5 1.0 N A:CYS252 3.7 38.1 1.0 CA A:CYS252 4.1 38.4 1.0 CE1 A:PHE182 4.2 36.8 1.0 N A:CYS272 4.2 41.6 1.0 CA A:CYS272 4.5 41.4 1.0 CB A:ARG251 4.5 38.6 1.0 CA A:CYS249 4.6 39.7 1.0 CZ A:PHE182 4.7 39.5 1.0 C A:ARG251 4.7 39.2 1.0 CA A:CYS269 4.8 39.1 1.0 C A:CYS252 4.8 40.7 1.0 CB A:THR254 4.8 40.6 1.0 N A:GLY253 5.0 42.0 1.0 CA A:ARG251 5.0 38.9 1.0 N A:ARG251 5.0 39.8 1.0 CB A:ARG271 5.0 43.4 1.0 O A:THR254 5.0 40.5 1.0

A.Banerjee, W.L.Santos, G.L.Verdine. Structure of A Dna Glycosylase Searching For Lesions. Science V. 311 1153 2006.
ISSN: ISSN 0036-8075
PubMed: 16497933
DOI: 10.1126/SCIENCE.1120288