Zinc in PDB 5lfy: Zinc Bound Dimer of the Fragment of Human Amyloid-Beta Peptide with Alzheimer'S Disease Pathogenic Taiwanese Mutation D7H

The binding sites of Zinc atom in the Zinc Bound Dimer of the Fragment of Human Amyloid-Beta Peptide with Alzheimer'S Disease Pathogenic Taiwanese Mutation D7H (pdb code 5lfy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Zinc Bound Dimer of the Fragment of Human Amyloid-Beta Peptide with Alzheimer'S Disease Pathogenic Taiwanese Mutation D7H, PDB code: 5lfy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Zinc Bound Dimer of the Fragment of Human Amyloid-Beta Peptide with Alzheimer'S Disease Pathogenic Taiwanese Mutation D7H


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zinc Bound Dimer of the Fragment of Human Amyloid-Beta Peptide with Alzheimer'S Disease Pathogenic Taiwanese Mutation D7H within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:0.0 occ:1.00 OE1 A:GLU3 2.0 0.0 1.0 NE2 A:HIS7 2.0 0.0 1.0 O B:ASP1 2.0 0.0 1.0 NE2 B:HIS6 2.1 0.0 1.0 CD A:GLU3 2.3 0.0 1.0 OE2 A:GLU3 2.4 0.0 1.0 CD2 A:HIS7 2.9 0.0 1.0 HA B:ALA2 2.9 0.0 1.0 HD2 A:HIS7 3.0 0.0 1.0 CE1 B:HIS6 3.0 0.0 1.0 C B:ASP1 3.0 0.0 1.0 HE1 B:HIS6 3.1 0.0 1.0 CE1 A:HIS7 3.2 0.0 1.0 CD2 B:HIS6 3.2 0.0 1.0 HD2 B:HIS6 3.5 0.0 1.0 HE1 A:HIS7 3.5 0.0 1.0 CG A:GLU3 3.6 0.0 1.0 HA A:GLU3 3.6 0.0 1.0 HG3 A:GLU3 3.6 0.0 1.0 CA B:ALA2 3.7 0.0 1.0 N B:ALA2 3.7 0.0 1.0 H1 B:ASP1 3.7 0.0 1.0 HB2 A:HIS6 3.8 0.0 1.0 H2 B:ASP1 3.8 0.0 1.0 HB2 B:ASP1 4.0 0.0 1.0 CA B:ASP1 4.0 0.0 1.0 N B:ASP1 4.1 0.0 1.0 CG A:HIS7 4.1 0.0 1.0 C B:ALA2 4.1 0.0 1.0 ND1 B:HIS6 4.2 0.0 1.0 HD2 A:HIS6 4.2 0.0 1.0 ND1 A:HIS7 4.2 0.0 1.0 CG B:HIS6 4.3 0.0 1.0 HG2 A:GLU3 4.3 0.0 1.0 CB A:GLU3 4.4 0.0 1.0 CA A:GLU3 4.5 0.0 1.0 O B:ALA2 4.5 0.0 1.0 H B:ALA2 4.5 0.0 1.0 CB B:ASP1 4.6 0.0 1.0 HB3 A:HIS6 4.6 0.0 1.0 HB2 A:GLU3 4.6 0.0 1.0 CB A:HIS6 4.6 0.0 1.0 N B:GLU3 4.7 0.0 1.0 H B:GLU3 4.7 0.0 1.0 CD2 A:HIS6 4.8 0.0 1.0 O A:GLU3 4.9 0.0 1.0 HA B:ASP1 4.9 0.0 1.0 CB B:ALA2 5.0 0.0 1.0

Zinc binding site 2 out of 2 in the Zinc Bound Dimer of the Fragment of Human Amyloid-Beta Peptide with Alzheimer'S Disease Pathogenic Taiwanese Mutation D7H


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zinc Bound Dimer of the Fragment of Human Amyloid-Beta Peptide with Alzheimer'S Disease Pathogenic Taiwanese Mutation D7H within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn102 b:0.0 occ:1.00 OE1 B:GLU3 2.0 0.0 1.0 NE2 B:HIS7 2.0 0.0 1.0 O A:ASP1 2.0 0.0 1.0 NE2 A:HIS6 2.1 0.0 1.0 CD B:GLU3 2.1 0.0 1.0 OE2 B:GLU3 2.2 0.0 1.0 HA A:ALA2 2.7 0.0 1.0 CE1 A:HIS6 2.9 0.0 1.0 CD2 B:HIS7 3.0 0.0 1.0 C A:ASP1 3.0 0.0 1.0 HE1 A:HIS6 3.1 0.0 1.0 CE1 B:HIS7 3.1 0.0 1.0 HD2 B:HIS7 3.1 0.0 1.0 CD2 A:HIS6 3.2 0.0 1.0 CG B:GLU3 3.4 0.0 1.0 HE1 B:HIS7 3.4 0.0 1.0 HG3 B:GLU3 3.4 0.0 1.0 CA A:ALA2 3.5 0.0 1.0 HD2 A:HIS6 3.5 0.0 1.0 HA B:GLU3 3.5 0.0 1.0 N A:ALA2 3.6 0.0 1.0 HB2 A:ASP1 3.9 0.0 1.0 HB2 B:HIS6 4.0 0.0 1.0 H3 A:ASP1 4.0 0.0 1.0 C A:ALA2 4.0 0.0 1.0 CA A:ASP1 4.1 0.0 1.0 HG2 B:GLU3 4.1 0.0 1.0 ND1 A:HIS6 4.1 0.0 1.0 CG B:HIS7 4.2 0.0 1.0 ND1 B:HIS7 4.2 0.0 1.0 CB B:GLU3 4.2 0.0 1.0 CG A:HIS6 4.3 0.0 1.0 H1 A:ASP1 4.3 0.0 1.0 HB2 B:GLU3 4.3 0.0 1.0 CA B:GLU3 4.4 0.0 1.0 N A:ASP1 4.4 0.0 1.0 HD2 B:HIS6 4.4 0.0 1.0 O A:ALA2 4.5 0.0 1.0 CB A:ASP1 4.5 0.0 1.0 H A:ALA2 4.5 0.0 1.0 N A:GLU3 4.6 0.0 1.0 H A:GLU3 4.6 0.0 1.0 HB3 A:ASP1 4.7 0.0 1.0 CB A:ALA2 4.8 0.0 1.0 HB3 A:ALA2 4.8 0.0 1.0 HB3 B:HIS6 4.8 0.0 1.0 CB B:HIS6 4.8 0.0 1.0 O B:GLU3 4.8 0.0 1.0 HD1 A:HIS6 5.0 0.0 1.0

V.I.Polshakov, A.B.Mantsyzov, S.A.Kozin, A.A.Adzhubei, S.S.Zhokhov, W.Van Beek, A.A.Kulikova, M.I.Indeykina, V.A.Mitkevich, A.A.Makarov. A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer'S Amyloid-Beta Fragment with Taiwanese Mutation D7H. Angew. Chem. Int. Ed. Engl. V. 56 11734 2017.
ISSN: ESSN 1521-3773
PubMed: 28570778
DOI: 10.1002/ANIE.201704615