Zinc in PDB 1u8b: Crystal Structure of the Methylated N-Ada/Dna Complex

The structure of Crystal Structure of the Methylated N-Ada/Dna Complex, PDB code: 1u8b was solved by C.He, J.-C.Hus, L.J.Sun, P.Zhou, D.P.G.Norman, V.Dotsch, J.D.Gross, W.S.Lane, G.Wagner, G.L.Verdine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.40 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	28.842, 84.593, 108.357, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 27.4

The binding sites of Zinc atom in the Crystal Structure of the Methylated N-Ada/Dna Complex (pdb code 1u8b). 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 the Methylated N-Ada/Dna Complex, PDB code: 1u8b:

Zinc binding site 1 out of 1 in the Crystal Structure of the Methylated N-Ada/Dna Complex


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 the Methylated N-Ada/Dna Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn150 b:29.5 occ:1.00 SG A:CYS72 2.2 34.8 1.0 SG A:CYS69 2.3 32.2 1.0 SG A:CYS42 2.3 28.5 1.0 SG A:SMC38 2.5 34.1 1.0 CB A:CYS69 2.7 32.8 1.0 CB A:SMC38 3.0 32.4 1.0 CS A:SMC38 3.1 33.6 1.0 CB A:CYS42 3.2 26.6 1.0 CB A:CYS72 3.3 33.1 1.0 N A:CYS72 3.7 34.1 1.0 CA A:SMC38 4.0 31.1 1.0 CA A:CYS72 4.1 34.1 1.0 CA A:CYS69 4.2 34.6 1.0 CB A:ARG71 4.5 36.2 1.0 CA A:CYS42 4.5 29.2 1.0 C A:ARG71 4.6 34.7 1.0 N A:ARG71 4.6 34.8 1.0 N A:ARG39 4.6 32.3 1.0 C A:CYS69 4.7 33.7 1.0 CA A:ARG71 4.8 34.7 1.0 O A:PHE37 4.9 26.2 1.0 C A:SMC38 4.9 32.3 1.0 N A:SMC38 4.9 30.4 1.0 N A:CYS69 5.0 35.0 1.0

C.He, J.C.Hus, L.J.Sun, P.Zhou, D.P.Norman, V.Dotsch, H.Wei, J.D.Gross, W.S.Lane, G.Wagner, G.L.Verdine. A Methylation-Dependent Electrostatic Switch Controls Dna Repair and Transcriptional Activation By E. Coli Ada. Mol.Cell V. 20 117 2005.
ISSN: ISSN 1097-2765
PubMed: 16209950
DOI: 10.1016/J.MOLCEL.2005.08.013