Zinc in PDB 1co4: Solution Structure of A Zinc Domain Conserved in Yeast Copper-Regulated Transcription Factors

The binding sites of Zinc atom in the Solution Structure of A Zinc Domain Conserved in Yeast Copper-Regulated Transcription Factors (pdb code 1co4). 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 Solution Structure of A Zinc Domain Conserved in Yeast Copper-Regulated Transcription Factors, PDB code: 1co4:

Zinc binding site 1 out of 1 in the Solution Structure of A Zinc Domain Conserved in Yeast Copper-Regulated Transcription Factors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of A Zinc Domain Conserved in Yeast Copper-Regulated Transcription Factors within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn43 b:1.0 occ:1.00 ND1 A:HIS25 2.1 1.0 1.0 SG A:CYS23 2.3 1.0 1.0 SG A:CYS11 2.3 1.0 1.0 SG A:CYS14 2.4 1.0 1.0 CE1 A:HIS25 2.9 1.0 1.0 HE1 A:HIS25 3.1 1.0 1.0 CB A:CYS23 3.1 1.0 1.0 H A:HIS25 3.1 1.0 1.0 CG A:HIS25 3.2 1.0 1.0 HB3 A:CYS11 3.2 1.0 1.0 CB A:CYS14 3.3 1.0 1.0 CB A:CYS11 3.4 1.0 1.0 H A:CYS11 3.5 1.0 1.0 H A:GLU24 3.6 1.0 1.0 HA A:CYS23 3.6 1.0 1.0 CB A:HIS25 3.6 1.0 1.0 CA A:CYS23 3.9 1.0 1.0 HB3 A:CYS14 3.9 1.0 1.0 HB3 A:CYS23 4.0 1.0 1.0 N A:HIS25 4.0 1.0 1.0 NE2 A:HIS25 4.1 1.0 1.0 N A:GLU24 4.2 1.0 1.0 CD2 A:HIS25 4.2 1.0 1.0 N A:CYS11 4.3 1.0 1.0 CA A:CYS11 4.4 1.0 1.0 CA A:HIS25 4.4 1.0 1.0 C A:CYS23 4.5 1.0 1.0 HB3 A:HIS25 4.5 1.0 1.0 CA A:CYS14 4.5 1.0 1.0 O A:SER13 4.5 1.0 1.0 N A:CYS14 4.6 1.0 1.0 C A:SER13 4.6 1.0 1.0 HA A:ALA20 4.6 1.0 1.0 HA A:CYS14 4.8 1.0 1.0 H A:SER13 4.8 1.0 1.0 HB3 A:SER13 4.9 1.0 1.0 NH2 A:ARG28 4.9 1.0 1.0 HB3 A:LYS19 4.9 1.0 1.0 HE A:ARG28 4.9 1.0 1.0 HE2 A:HIS25 5.0 1.0 1.0

R.B.Turner, D.L.Smith, M.E.Zawrotny, M.F.Summers, M.C.Posewitz, D.R.Winge. Solution Structure of A Zinc Domain Conserved in Yeast Copper-Regulated Transcription Factors. Nat.Struct.Biol. V. 5 551 1998.
ISSN: ISSN 1072-8368
PubMed: 9665167
DOI: 10.1038/805