Zinc in PDB 1kmg: The Solution Structure of Monomeric Copper-Free Superoxide Dismutase

All present enzymatic activity of The Solution Structure of Monomeric Copper-Free Superoxide Dismutase:
1.15.1.1;

The binding sites of Zinc atom in the The Solution Structure of Monomeric Copper-Free Superoxide Dismutase (pdb code 1kmg). 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 The Solution Structure of Monomeric Copper-Free Superoxide Dismutase, PDB code: 1kmg:

Zinc binding site 1 out of 1 in the The Solution Structure of Monomeric Copper-Free Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Solution Structure of Monomeric Copper-Free Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn154 b:0.4 occ:1.00 O A:THR137 1.9 0.3 1.0 OD2 A:ASP83 1.9 1.7 1.0 ND1 A:HIS71 2.1 0.4 1.0 ND1 A:HIS80 2.2 0.4 1.0 ND1 A:HIS63 2.2 0.4 1.0 CG A:ASP83 2.7 0.8 1.0 CE1 A:HIS71 3.1 0.5 1.0 CG A:HIS71 3.1 0.4 1.0 C A:THR137 3.1 0.3 1.0 CE1 A:HIS80 3.1 0.4 1.0 HA A:HIS71 3.1 0.7 1.0 OD1 A:ASP83 3.2 2.2 1.0 CE1 A:HIS63 3.2 0.5 1.0 CG A:HIS80 3.2 0.5 1.0 HB2 A:HIS63 3.3 0.6 1.0 CG A:HIS63 3.3 0.4 1.0 HE1 A:HIS71 3.3 0.5 1.0 HE1 A:HIS80 3.3 0.4 1.0 HB2 A:HIS71 3.3 0.4 1.0 HE1 A:HIS63 3.4 0.6 1.0 HA3 A:GLY138 3.4 0.4 1.0 H A:HIS80 3.5 0.6 1.0 HB2 A:HIS80 3.5 0.6 1.0 CB A:HIS71 3.6 0.4 1.0 HB3 A:ASP83 3.6 2.3 1.0 HA A:THR137 3.7 0.4 1.0 CB A:HIS63 3.7 0.5 1.0 CB A:ASP83 3.8 1.1 1.0 CA A:HIS71 3.8 0.6 1.0 CB A:HIS80 3.9 0.6 1.0 HB3 A:HIS63 3.9 0.6 1.0 N A:GLY138 4.0 0.3 1.0 CA A:THR137 4.0 0.4 1.0 CA A:GLY138 4.1 0.3 1.0 H A:GLY72 4.1 1.0 1.0 NE2 A:HIS80 4.1 0.4 1.0 NE2 A:HIS71 4.2 0.5 1.0 HB2 A:ASP83 4.2 2.3 1.0 CD2 A:HIS80 4.2 0.5 1.0 CD2 A:HIS71 4.2 0.5 1.0 N A:HIS80 4.2 0.5 1.0 HA2 A:GLY138 4.2 0.4 1.0 NE2 A:HIS63 4.3 0.6 1.0 HB A:THR137 4.4 0.8 1.0 CD2 A:HIS63 4.4 0.5 1.0 HB3 A:HIS71 4.6 0.5 1.0 CA A:HIS80 4.6 0.5 1.0 N A:HIS71 4.6 0.6 1.0 HB3 A:HIS80 4.8 0.7 1.0 CB A:THR137 4.8 0.5 1.0 H A:HIS63 4.9 0.9 1.0 N A:GLY72 4.9 0.8 1.0 H A:GLY138 4.9 0.4 1.0 C A:HIS71 5.0 0.8 1.0 HE2 A:HIS80 5.0 0.4 1.0

L.Banci, I.Bertini, F.Cantini, M.D'onofrio, M.S.Viezzoli. Structure and Dynamics of Copper-Free Sod: the Protein Before Binding Copper. Protein Sci. V. 11 2479 2002.
ISSN: ISSN 0961-8368
PubMed: 12237469
DOI: 10.1110/PS.0210802