Zinc in PDB 2ld1: Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein

All present enzymatic activity of Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein:
3.6.4.12;

The binding sites of Zinc atom in the Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein (pdb code 2ld1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein, PDB code: 2ld1:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:0.0 occ:1.00 SG A:CYS200 2.3 0.0 1.0 SG A:CYS174 2.3 0.0 1.0 SG A:CYS171 2.3 0.0 1.0 SG A:CYS197 2.3 0.0 1.0 H A:CYS197 2.8 0.0 1.0 HB2 A:CYS200 3.2 0.0 1.0 HB2 A:CYS174 3.3 0.0 1.0 CB A:CYS171 3.4 0.0 1.0 CB A:CYS200 3.4 0.0 1.0 CB A:CYS174 3.4 0.0 1.0 HB3 A:CYS197 3.5 0.0 1.0 H A:CYS174 3.5 0.0 1.0 CB A:CYS197 3.5 0.0 1.0 HB3 A:CYS171 3.5 0.0 1.0 HB2 A:CYS171 3.6 0.0 1.0 N A:CYS197 3.6 0.0 1.0 HB3 A:ALA173 3.7 0.0 1.0 HB A:ILE196 3.8 0.0 1.0 H A:CYS200 3.9 0.0 1.0 N A:CYS174 4.0 0.0 1.0 CA A:CYS197 4.2 0.0 1.0 HB3 A:CYS200 4.2 0.0 1.0 HB3 A:CYS174 4.2 0.0 1.0 N A:CYS200 4.3 0.0 1.0 CA A:CYS200 4.3 0.0 1.0 CA A:CYS174 4.4 0.0 1.0 HB2 A:CYS197 4.4 0.0 1.0 HA A:CYS200 4.5 0.0 1.0 HB2 A:ALA173 4.5 0.0 1.0 HB2 A:ASN199 4.5 0.0 1.0 CB A:ALA173 4.5 0.0 1.0 HA A:ILE196 4.5 0.0 1.0 O A:CYS197 4.6 0.0 1.0 H A:ALA173 4.6 0.0 1.0 C A:ILE196 4.6 0.0 1.0 C A:ALA173 4.7 0.0 1.0 C A:CYS197 4.7 0.0 1.0 CB A:ILE196 4.8 0.0 1.0 CA A:CYS171 4.8 0.0 1.0 HA A:CYS174 4.8 0.0 1.0 CA A:ILE196 4.9 0.0 1.0

Zinc binding site 2 out of 3 in the Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:0.0 occ:1.00 SG A:CYS220 2.3 0.0 1.0 SG A:CYS240 2.3 0.0 1.0 SG A:CYS243 2.3 0.0 1.0 SG A:CYS223 2.3 0.0 1.0 H A:CYS223 2.9 0.0 1.0 HB2 A:CYS243 3.2 0.0 1.0 CB A:CYS220 3.3 0.0 1.0 HB2 A:CYS220 3.3 0.0 1.0 HB3 A:CYS223 3.4 0.0 1.0 HB3 A:CYS240 3.4 0.0 1.0 CB A:CYS243 3.4 0.0 1.0 H A:CYS240 3.4 0.0 1.0 CB A:CYS223 3.5 0.0 1.0 CB A:CYS240 3.5 0.0 1.0 HB3 A:CYS220 3.5 0.0 1.0 HB3 A:TRP222 3.6 0.0 1.0 N A:CYS223 3.8 0.0 1.0 H A:CYS243 3.9 0.0 1.0 HB2 A:GLU225 4.1 0.0 1.0 N A:CYS240 4.1 0.0 1.0 HB3 A:CYS243 4.1 0.0 1.0 CA A:CYS223 4.2 0.0 1.0 N A:CYS243 4.3 0.0 1.0 HB2 A:TRP222 4.3 0.0 1.0 HB2 A:CYS240 4.3 0.0 1.0 H A:ALA224 4.3 0.0 1.0 HB2 A:CYS223 4.3 0.0 1.0 HB2 A:LYS242 4.4 0.0 1.0 CA A:CYS240 4.4 0.0 1.0 CA A:CYS243 4.4 0.0 1.0 CB A:TRP222 4.4 0.0 1.0 HD1 A:PHE239 4.4 0.0 1.0 H A:TRP222 4.4 0.0 1.0 H A:GLU225 4.5 0.0 1.0 HA A:CYS243 4.7 0.0 1.0 HG3 A:GLU225 4.7 0.0 1.0 CA A:CYS220 4.7 0.0 1.0 O A:CYS240 4.8 0.0 1.0 N A:ALA224 4.8 0.0 1.0 C A:TRP222 4.8 0.0 1.0 C A:CYS240 4.9 0.0 1.0 C A:CYS223 4.9 0.0 1.0 HA A:CYS220 4.9 0.0 1.0 HA A:ALA173 4.9 0.0 1.0 N A:TRP222 5.0 0.0 1.0 H A:GLY226 5.0 0.0 1.0

Zinc binding site 3 out of 3 in the Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structures and Chemical Shift Assignments For the Add Domain of the Atrx Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3 b:0.0 occ:1.00 SG A:CYS232 2.3 0.0 1.0 SG A:CYS265 2.3 0.0 1.0 SG A:CYS235 2.3 0.0 1.0 SG A:CYS268 2.3 0.0 1.0 H A:CYS235 2.7 0.0 1.0 H A:CYS268 3.1 0.0 1.0 HB3 A:CYS235 3.2 0.0 1.0 HB2 A:PHE234 3.3 0.0 1.0 H A:CYS265 3.3 0.0 1.0 CB A:CYS232 3.4 0.0 1.0 CB A:CYS235 3.4 0.0 1.0 HB2 A:CYS232 3.5 0.0 1.0 HB3 A:CYS232 3.5 0.0 1.0 HB A:ILE267 3.5 0.0 1.0 N A:CYS235 3.5 0.0 1.0 HB2 A:CYS268 3.5 0.0 1.0 CB A:CYS268 3.5 0.0 1.0 HB3 A:CYS265 3.6 0.0 1.0 CB A:CYS265 3.6 0.0 1.0 N A:CYS268 3.8 0.0 1.0 N A:CYS265 4.0 0.0 1.0 CA A:CYS235 4.1 0.0 1.0 CA A:CYS268 4.2 0.0 1.0 CB A:PHE234 4.2 0.0 1.0 H A:PHE234 4.2 0.0 1.0 HB3 A:PHE234 4.2 0.0 1.0 HB2 A:CYS235 4.3 0.0 1.0 HA A:CYS268 4.3 0.0 1.0 CA A:CYS265 4.4 0.0 1.0 HB3 A:CYS268 4.4 0.0 1.0 HB2 A:CYS265 4.4 0.0 1.0 HA A:TYR264 4.5 0.0 1.0 HB2 A:ASN237 4.5 0.0 1.0 H A:ILE267 4.5 0.0 1.0 CB A:ILE267 4.6 0.0 1.0 C A:PHE234 4.6 0.0 1.0 HE2 A:PHE239 4.6 0.0 1.0 HD2 A:PHE234 4.6 0.0 1.0 CA A:CYS232 4.7 0.0 1.0 C A:ILE267 4.8 0.0 1.0 N A:PHE234 4.8 0.0 1.0 C A:CYS235 4.8 0.0 1.0 CA A:PHE234 4.8 0.0 1.0 C A:CYS265 4.9 0.0 1.0 N A:ILE267 4.9 0.0 1.0 O A:TRP263 4.9 0.0 1.0 C A:TYR264 5.0 0.0 1.0 HA A:CYS235 5.0 0.0 1.0

A.Argentaro, J.C.Yang, L.Chapman, M.S.Kowalczyk, R.J.Gibbons, D.R.Higgs, D.Neuhaus, D.Rhodes. Structural Consequences of Disease-Causing Mutations in the Atrx-DNMT3-DNMT3L (Add) Domain of the Chromatin-Associated Protein Atrx. Proc.Natl.Acad.Sci.Usa V. 104 11939 2007.
ISSN: ISSN 0027-8424
PubMed: 17609377
DOI: 10.1073/PNAS.0704057104