Zinc in PDB 2af2: Solution Structure of Disulfide Reduced and Copper Depleted Human Superoxide Dismutase

All present enzymatic activity of Solution Structure of Disulfide Reduced and Copper Depleted Human Superoxide Dismutase:
1.15.1.1;

The binding sites of Zinc atom in the Solution Structure of Disulfide Reduced and Copper Depleted Human Superoxide Dismutase (pdb code 2af2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of Disulfide Reduced and Copper Depleted Human Superoxide Dismutase, PDB code: 2af2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Solution Structure of Disulfide Reduced and Copper Depleted Human Superoxide Dismutase


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 Disulfide Reduced and Copper Depleted Human Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn154 b:0.0 occ:1.00 OD1 A:ASP83 2.0 0.0 1.0 ND1 A:HIS63 2.1 0.0 1.0 ND1 A:HIS71 2.1 0.0 1.0 ND1 A:HIS80 2.1 0.0 1.0 OD2 A:ASP83 2.3 0.0 1.0 CG A:ASP83 2.4 0.0 1.0 CE1 A:HIS63 2.9 0.0 1.0 CE1 A:HIS71 3.0 0.0 1.0 HA A:HIS71 3.0 0.0 1.0 HB2 A:HIS80 3.0 0.0 1.0 CE1 A:HIS80 3.1 0.0 1.0 HE1 A:HIS63 3.1 0.0 1.0 HE1 A:HIS71 3.1 0.0 1.0 CG A:HIS80 3.2 0.0 1.0 CG A:HIS71 3.2 0.0 1.0 CG A:HIS63 3.2 0.0 1.0 HB2 A:HIS63 3.2 0.0 1.0 HE1 A:HIS80 3.3 0.0 1.0 HB2 A:HIS71 3.6 0.0 1.0 CB A:HIS80 3.6 0.0 1.0 CB A:HIS71 3.7 0.0 1.0 H A:GLY72 3.7 0.0 1.0 CB A:HIS63 3.8 0.0 1.0 CA A:HIS71 3.8 0.0 1.0 HD2 A:HIS46 3.9 0.0 1.0 CB A:ASP83 3.9 0.0 1.0 H A:HIS80 4.0 0.0 1.0 CD2 A:HIS46 4.1 0.0 1.0 NE2 A:HIS63 4.1 0.0 1.0 NE2 A:HIS71 4.1 0.0 1.0 HB3 A:HIS46 4.2 0.0 1.0 NE2 A:HIS80 4.2 0.0 1.0 CD2 A:HIS71 4.2 0.0 1.0 CD2 A:HIS63 4.3 0.0 1.0 CD2 A:HIS80 4.3 0.0 1.0 HB3 A:HIS80 4.3 0.0 1.0 HB3 A:ASP83 4.3 0.0 1.0 HB3 A:HIS63 4.4 0.0 1.0 HB2 A:ASP83 4.5 0.0 1.0 CG A:HIS46 4.5 0.0 1.0 HA A:ASP83 4.6 0.0 1.0 O A:GLY82 4.6 0.0 1.0 N A:GLY72 4.6 0.0 1.0 NE2 A:HIS46 4.7 0.0 1.0 CA A:ASP83 4.7 0.0 1.0 N A:HIS80 4.8 0.0 1.0 C A:HIS71 4.8 0.0 1.0 H A:HIS63 4.8 0.0 1.0 O A:LYS136 4.8 0.0 1.0 C A:GLY82 4.8 0.0 1.0 N A:HIS71 4.8 0.0 1.0 HB3 A:HIS71 4.8 0.0 1.0 CA A:HIS80 4.8 0.0 1.0 O A:HIS63 4.8 0.0 1.0 HA A:THR137 4.8 0.0 1.0 N A:ASP83 4.9 0.0 1.0 CB A:HIS46 4.9 0.0 1.0 CA A:HIS63 5.0 0.0 1.0 HE2 A:HIS63 5.0 0.0 1.0

Zinc binding site 2 out of 2 in the Solution Structure of Disulfide Reduced and Copper Depleted Human Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of Disulfide Reduced and Copper Depleted Human Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn154 b:0.0 occ:1.00 OD2 B:ASP83 2.0 0.0 1.0 ND1 B:HIS63 2.1 0.0 1.0 ND1 B:HIS71 2.1 0.0 1.0 ND1 B:HIS80 2.2 0.0 1.0 HB3 B:ASP83 2.7 0.0 1.0 CG B:ASP83 2.9 0.0 1.0 CE1 B:HIS63 3.0 0.0 1.0 CE1 B:HIS71 3.0 0.0 1.0 HB2 B:ASP83 3.1 0.0 1.0 CB B:ASP83 3.1 0.0 1.0 HE1 B:HIS63 3.1 0.0 1.0 CG B:HIS71 3.2 0.0 1.0 CG B:HIS63 3.2 0.0 1.0 CE1 B:HIS80 3.2 0.0 1.0 HA B:HIS71 3.2 0.0 1.0 HB2 B:HIS80 3.2 0.0 1.0 HB2 B:HIS63 3.2 0.0 1.0 HE1 B:HIS71 3.2 0.0 1.0 CG B:HIS80 3.3 0.0 1.0 HE1 B:HIS80 3.4 0.0 1.0 HB2 B:HIS71 3.5 0.0 1.0 H B:HIS80 3.7 0.0 1.0 CB B:HIS71 3.7 0.0 1.0 CB B:HIS63 3.8 0.0 1.0 CB B:HIS80 3.8 0.0 1.0 CA B:HIS71 4.0 0.0 1.0 H B:GLY72 4.0 0.0 1.0 O B:THR137 4.0 0.0 1.0 OD1 B:ASP83 4.1 0.0 1.0 NE2 B:HIS63 4.1 0.0 1.0 NE2 B:HIS71 4.2 0.0 1.0 CD2 B:HIS63 4.2 0.0 1.0 CD2 B:HIS71 4.2 0.0 1.0 NE2 B:HIS80 4.3 0.0 1.0 O B:HIS63 4.3 0.0 1.0 CD2 B:HIS80 4.4 0.0 1.0 HB3 B:HIS63 4.4 0.0 1.0 HB3 B:HIS80 4.5 0.0 1.0 N B:HIS80 4.5 0.0 1.0 HD2 B:HIS46 4.6 0.0 1.0 CA B:ASP83 4.6 0.0 1.0 HB3 B:HIS71 4.7 0.0 1.0 N B:GLY72 4.8 0.0 1.0 CA B:HIS80 4.8 0.0 1.0 O B:GLY82 4.9 0.0 1.0 CA B:HIS63 4.9 0.0 1.0 H B:HIS63 4.9 0.0 1.0 CD2 B:HIS46 4.9 0.0 1.0 N B:HIS71 4.9 0.0 1.0 HA B:ARG79 4.9 0.0 1.0 C B:HIS63 4.9 0.0 1.0 C B:HIS71 5.0 0.0 1.0

L.Banci, I.Bertini, F.Cantini, N.D'amelio, E.Gaggelli. Human SOD1 Before Harboring the Catalytic Metal: Solution Structure of Copper-Depleted, Disulfide-Reduced Form J.Biol.Chem. V. 281 2333 2006.
ISSN: ISSN 0021-9258
PubMed: 16291742
DOI: 10.1074/JBC.M506497200