Zinc in PDB 1hl4: The Structure of Apo Type Human Cu, Zn Superoxide Dismutase

All present enzymatic activity of The Structure of Apo Type Human Cu, Zn Superoxide Dismutase:
1.15.1.1;

The structure of The Structure of Apo Type Human Cu, Zn Superoxide Dismutase, PDB code: 1hl4 was solved by R.W.Strange, S.Antonyuk, M.A.Hough, P.Doucette, J.Rodriguez, P.J.Hart, L.J.Hayward, J.S.Valentine, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.82
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	156.404, 34.978, 114.809, 90.00, 112.26, 90.00
R / Rfree (%)	23.2 / 28.3

The binding sites of Zinc atom in the The Structure of Apo Type Human Cu, Zn Superoxide Dismutase (pdb code 1hl4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structure of Apo Type Human Cu, Zn Superoxide Dismutase, PDB code: 1hl4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Structure of Apo Type Human Cu, Zn 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 Structure of Apo Type Human Cu, Zn Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn155 b:32.3 occ:0.20 ND1 A:HIS80 1.9 25.7 1.0 ND1 A:HIS63 2.0 27.9 1.0 OD1 A:ASP83 2.1 25.4 1.0 ND1 A:HIS71 2.4 26.4 1.0 CE1 A:HIS80 2.7 20.9 1.0 CE1 A:HIS63 2.8 26.4 1.0 CG A:HIS80 2.9 24.6 1.0 CG A:ASP83 3.1 18.7 1.0 CG A:HIS63 3.1 22.1 1.0 OD2 A:ASP83 3.3 25.6 1.0 CE1 A:HIS71 3.3 19.8 1.0 CG A:HIS71 3.4 24.2 1.0 CB A:HIS80 3.5 24.3 1.0 CB A:HIS63 3.6 21.6 1.0 CB A:HIS71 3.7 23.8 1.0 NE2 A:HIS80 3.7 26.5 1.0 CD2 A:HIS80 3.9 23.1 1.0 NE2 A:HIS63 3.9 26.3 1.0 O A:LYS136 4.0 29.9 1.0 CD2 A:HIS63 4.1 22.8 1.0 CA A:HIS71 4.2 25.2 1.0 NE2 A:HIS71 4.4 26.4 1.0 CB A:ASP83 4.4 21.2 1.0 CD2 A:HIS71 4.5 25.0 1.0 CA A:HIS80 4.7 25.4 1.0 CA A:ASP83 4.7 20.8 1.0 N A:HIS80 4.8 25.5 1.0 N A:ASP83 4.9 23.1 1.0 C A:LYS136 5.0 29.0 1.0

Zinc binding site 2 out of 2 in the The Structure of Apo Type Human Cu, Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of Apo Type Human Cu, Zn Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn155 b:37.7 occ:0.20 OD1 B:ASP83 1.9 25.5 1.0 ND1 B:HIS63 2.0 28.2 1.0 ND1 B:HIS80 2.0 23.5 1.0 ND1 B:HIS71 2.2 26.8 1.0 CE1 B:HIS63 2.6 25.8 1.0 CE1 B:HIS80 2.7 21.2 1.0 CG B:ASP83 2.8 19.9 1.0 OD2 B:ASP83 2.9 26.0 1.0 CE1 B:HIS71 3.0 27.9 1.0 CG B:HIS80 3.1 20.8 1.0 CG B:HIS63 3.2 24.6 1.0 CG B:HIS71 3.3 26.3 1.0 CB B:HIS80 3.7 22.1 1.0 CB B:HIS71 3.7 26.0 1.0 NE2 B:HIS63 3.8 30.9 1.0 CB B:HIS63 3.9 24.2 1.0 NE2 B:HIS80 3.9 25.9 1.0 O B:LYS136 4.0 29.2 1.0 CD2 B:HIS80 4.1 24.4 1.0 NE2 B:HIS71 4.1 28.9 1.0 CD2 B:HIS63 4.1 27.3 1.0 CA B:HIS71 4.2 26.1 1.0 CB B:ASP83 4.2 22.4 1.0 CD2 B:HIS71 4.3 27.7 1.0 CA B:ASP83 4.6 21.7 1.0 N B:HIS80 4.8 25.8 1.0 N B:ASP83 4.8 22.6 1.0 CA B:HIS80 4.9 23.6 1.0 N B:GLY72 4.9 26.5 1.0

R.W.Strange, S.Antonyuk, M.A.Hough, P.Doucette, J.Rodriguez, P.J.Hart, L.J.Hayward, J.S.Valentine, S.S.Hasnain. The Structure of Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and Its Relevance to Familial Amyotrophic Lateral Sclerosis J.Mol.Biol. V. 328 877 2003.
ISSN: ISSN 0022-2836
PubMed: 12729761
DOI: 10.1016/S0022-2836(03)00355-3