Zinc in PDB 3hff: Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands

All present enzymatic activity of Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands:
1.15.1.1;

The structure of Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands, PDB code: 3hff was solved by K.Saraboji, A.Nordlund, L.Leinartait, M.Oliveberg, D.T.Logan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.13 / 2.20
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	36.670, 36.670, 144.390, 90.00, 90.00, 120.00
R / Rfree (%)	22.4 / 28.1

The binding sites of Zinc atom in the Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands (pdb code 3hff). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands, PDB code: 3hff:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in the Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn154 b:37.8 occ:1.00 NE2 A:HIS120 2.0 18.2 1.0 ND1 A:HIS46 2.0 21.1 1.0 O A:HOH211 2.1 18.8 1.0 O A:HOH212 2.4 9.3 1.0 CE1 A:HIS120 2.9 20.2 1.0 CE1 A:HIS46 3.0 23.2 1.0 CD2 A:HIS120 3.0 18.3 1.0 CG A:HIS46 3.0 25.3 1.0 CB A:HIS46 3.3 27.2 1.0 ND1 A:HIS120 4.0 20.7 1.0 NE2 A:HIS46 4.1 24.6 1.0 CG A:HIS120 4.1 21.1 1.0 CD2 A:HIS46 4.1 23.7 1.0 CG2 A:VAL81 4.5 37.7 1.0 CA A:HIS46 4.8 26.9 1.0 CB A:VAL81 4.8 38.4 1.0 CG1 A:VAL118 4.8 27.6 1.0 CB A:VAL118 4.9 27.4 1.0

Zinc binding site 2 out of 5 in the Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn155 b:62.9 occ:1.00 OD2 A:ASP90 1.8 31.9 1.0 O A:HOH208 2.4 21.6 1.0 OD1 A:ASP92 2.5 33.4 1.0 O A:HOH207 2.9 30.0 1.0 CG A:ASP90 2.9 31.4 1.0 CG A:ASP92 3.1 32.2 1.0 OD2 A:ASP92 3.1 31.6 1.0 OD1 A:ASP90 3.4 32.9 1.0 CB A:ASP90 4.2 30.9 1.0 CB A:VAL94 4.2 29.6 1.0 CG2 A:VAL94 4.4 28.9 1.0 CB A:ASP92 4.5 31.2 1.0 N A:ASP92 4.6 30.8 1.0 CA A:ASP92 5.0 30.9 1.0

Zinc binding site 3 out of 5 in the Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn156 b:41.8 occ:1.00 O A:HOH206 2.2 21.1 1.0 N A:ALA1 2.2 24.2 1.0 O A:ALA1 2.2 25.2 1.0 O A:HOH209 2.3 9.7 1.0 C A:ALA1 2.9 24.5 1.0 CA A:ALA1 3.0 24.5 1.0 CB A:ALA1 3.6 23.6 1.0 NZ A:LYS3 3.8 29.8 1.0 N A:THR2 4.2 24.4 1.0 CE A:LYS3 4.3 29.4 1.0 O A:HOH204 4.3 23.4 1.0 O A:HOH213 4.4 26.4 1.0 O A:HOH223 4.8 28.7 1.0 CA A:THR2 5.0 24.0 1.0

Zinc binding site 4 out of 5 in the Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn158 b:60.7 occ:1.00 NE2 A:HIS110 2.1 24.5 1.0 CE1 A:HIS110 2.6 25.5 1.0 O A:HOH222 2.8 18.1 1.0 CD2 A:HIS110 3.2 23.5 1.0 ND1 A:HIS110 3.8 24.2 1.0 CG A:HIS110 4.1 23.4 1.0 CB A:ASP109 4.3 23.6 1.0 OD1 A:ASP109 4.9 27.2 1.0

Zinc binding site 5 out of 5 in the Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn159 b:76.6 occ:1.00 O A:HOH219 1.9 29.2 1.0 OD2 A:ASP125 2.0 26.3 1.0 O A:HOH216 2.6 16.3 1.0 CG A:ASP125 2.7 27.0 1.0 OD1 A:ASP125 2.8 29.3 1.0 O A:HOH214 3.4 35.4 1.0 O A:HOH215 3.9 18.3 1.0 CB A:ASP125 4.2 25.9 1.0 N A:GLY129 4.3 21.7 1.0 CA A:GLY129 4.3 21.9 1.0 CA A:GLY127 4.7 23.9 1.0 N A:GLY127 4.8 24.3 1.0 N A:LYS128 5.0 23.6 1.0 C A:GLY127 5.0 23.7 1.0

A.Nordlund, L.Leinartaite, K.Saraboji, C.Aisenbrey, G.Grobner, P.Zetterstrom, J.Danielsson, D.T.Logan, M.Oliveberg. Functional Features Cause Misfolding of the Als-Provoking Enzyme SOD1. Proc.Natl.Acad.Sci.Usa V. 106 9667 2009.
ISSN: ISSN 0027-8424
PubMed: 19497878
DOI: 10.1073/PNAS.0812046106