Zinc in PDB 6pv2: Backbone-Modified Variant of Zinc Finger 2 From the Transcription Factor SP1 Dna Binding Domain: Orn in the Metal-Binding Turn

The binding sites of Zinc atom in the Backbone-Modified Variant of Zinc Finger 2 From the Transcription Factor SP1 Dna Binding Domain: Orn in the Metal-Binding Turn (pdb code 6pv2). 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 Backbone-Modified Variant of Zinc Finger 2 From the Transcription Factor SP1 Dna Binding Domain: Orn in the Metal-Binding Turn, PDB code: 6pv2:

Zinc binding site 1 out of 1 in the Backbone-Modified Variant of Zinc Finger 2 From the Transcription Factor SP1 Dna Binding Domain: Orn in the Metal-Binding Turn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Backbone-Modified Variant of Zinc Finger 2 From the Transcription Factor SP1 Dna Binding Domain: Orn in the Metal-Binding Turn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:0.2 occ:1.00 NE2 A:HIS22 2.0 0.1 1.0 NE2 A:HIS26 2.0 0.2 1.0 SG A:CYS9 2.3 0.2 1.0 SG A:CYS5 2.3 0.2 1.0 CE1 A:HIS22 3.0 0.2 1.0 CE1 A:HIS26 3.0 0.3 1.0 CD2 A:HIS22 3.0 0.1 1.0 CD2 A:HIS26 3.0 0.2 1.0 HB3 A:CYS9 3.1 0.3 1.0 HE1 A:HIS22 3.2 0.3 1.0 HE1 A:HIS26 3.2 0.3 1.0 HD2 A:HIS22 3.2 0.1 1.0 HD2 A:HIS26 3.2 0.2 1.0 CB A:CYS9 3.4 0.3 1.0 CB A:CYS5 3.4 0.1 1.0 HB3 A:CYS5 3.4 0.1 1.0 HB2 A:CYS5 3.5 0.2 1.0 HB3 A:TRP7 3.7 0.5 1.0 HB2 A:TRP7 3.9 0.4 1.0 HB2 A:CYS9 4.0 0.3 1.0 ND1 A:HIS22 4.1 0.2 1.0 HZ2 A:LYS23 4.1 2.4 1.0 O A:CYS9 4.1 0.3 1.0 ND1 A:HIS26 4.1 0.3 1.0 CG A:HIS22 4.1 0.1 1.0 CG A:HIS26 4.2 0.2 1.0 HD3 A:LYS23 4.2 1.4 1.0 H A:LYS11 4.3 0.2 1.0 H A:TRP7 4.3 0.5 1.0 CB A:TRP7 4.3 0.4 1.0 C A:CYS9 4.4 0.3 1.0 CA A:CYS9 4.5 0.3 1.0 HB2 A:LYS11 4.6 0.7 1.0 CA A:CYS5 4.8 0.2 1.0 HA A:LYS23 4.9 0.2 1.0 HG3 A:LYS11 4.9 1.2 1.0 HE2 A:PHE13 5.0 0.2 1.0 HD1 A:HIS22 5.0 0.2 1.0

S.R.Rao, W.S.Horne. Proteomimetic Zinc Finger Domains with Modified Metal-Binding Beta-Turns Peptide Science 2020.
ISSN: ISSN 1344-7661
DOI: 10.1002/PEP2.24177