Zinc in PDB 1ozu: Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution

All present enzymatic activity of Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution:
1.15.1.1;

The structure of Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution, PDB code: 1ozu was solved by J.S.Elam, A.B.Taylor, R.Strange, S.Antonyuk, P.A.Doucette, J.A.Rodriguez, S.S.Hasnain, L.J.Hayward, J.S.Valentine, T.O.Yeates, P.J.Hart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.70 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.086, 56.457, 105.350, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 19.3

The binding sites of Zinc atom in the Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution (pdb code 1ozu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution, PDB code: 1ozu:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn354 b:25.6 occ:1.00 NE2 A:HIS120 2.0 14.7 1.0 NE2 A:HIS48 2.0 12.4 1.0 ND1 A:HIS46 2.1 15.4 1.0 O4 A:SO4402 2.6 23.3 1.0 CE1 A:HIS48 2.8 12.9 1.0 CE1 A:HIS120 2.9 15.6 1.0 CD2 A:HIS120 3.0 14.8 1.0 CG A:HIS46 3.1 12.4 1.0 CE1 A:HIS46 3.1 15.7 1.0 CD2 A:HIS48 3.1 10.9 1.0 NE2 A:HIS63 3.3 14.8 1.0 CB A:HIS46 3.4 11.7 1.0 CD2 A:HIS63 3.6 14.8 1.0 S A:SO4402 3.8 22.3 1.0 O3 A:SO4402 3.9 24.1 1.0 ND1 A:HIS120 4.0 15.7 1.0 ND1 A:HIS48 4.0 11.8 1.0 CG A:HIS120 4.1 14.7 1.0 CG A:HIS48 4.2 9.9 1.0 NE2 A:HIS46 4.2 14.2 1.0 CD2 A:HIS46 4.2 13.2 1.0 CB A:VAL118 4.3 8.6 1.0 CG1 A:VAL118 4.3 9.7 1.0 CE1 A:HIS63 4.4 14.2 1.0 O2 A:SO4402 4.4 24.3 1.0 CA A:HIS46 4.6 9.9 1.0 CG A:HIS63 4.7 13.7 1.0 N A:HIS46 4.8 9.5 1.0 O A:HOH432 4.9 29.9 1.0 CG2 A:VAL118 4.9 9.0 1.0 O1 A:SO4402 4.9 25.9 1.0 O A:VAL118 5.0 10.1 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn355 b:14.8 occ:1.00 OD2 A:ASP83 1.9 13.9 1.0 ND1 A:HIS80 2.0 14.6 1.0 ND1 A:HIS71 2.1 14.6 1.0 ND1 A:HIS63 2.1 14.4 1.0 CG A:ASP83 2.7 13.1 1.0 OD1 A:ASP83 2.8 13.7 1.0 CE1 A:HIS80 2.9 15.0 1.0 CE1 A:HIS71 2.9 14.5 1.0 CE1 A:HIS63 3.0 14.2 1.0 CG A:HIS80 3.1 14.8 1.0 CG A:HIS63 3.1 13.7 1.0 CG A:HIS71 3.2 15.9 1.0 CB A:HIS63 3.5 13.2 1.0 CB A:HIS80 3.5 15.5 1.0 CB A:HIS71 3.6 17.9 1.0 O A:LYS136 3.9 30.2 1.0 CA A:HIS71 3.9 18.8 1.0 NE2 A:HIS80 4.0 16.1 1.0 NE2 A:HIS71 4.1 14.7 1.0 CD2 A:HIS80 4.1 15.4 1.0 NE2 A:HIS63 4.1 14.8 1.0 CB A:ASP83 4.1 12.6 1.0 CD2 A:HIS63 4.2 14.8 1.0 CD2 A:HIS71 4.2 15.3 1.0 N A:GLY72 4.6 18.5 1.0 N A:HIS80 4.7 16.6 1.0 CA A:ASP83 4.7 12.1 1.0 CA A:HIS80 4.7 15.6 1.0 C A:LYS136 4.8 30.3 1.0 C A:HIS71 4.8 18.7 1.0 N A:ASP83 4.9 11.8 1.0 O A:HOH433 4.9 24.9 1.0 N A:HIS71 4.9 19.8 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Familial Als Mutant S134N of Human Cu, Zn Superoxide Dismutase (Cuznsod) to 1.3A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn356 b:14.7 occ:1.00 O1 B:SO4401 1.8 21.4 1.0 NE2 B:HIS248 2.0 10.9 1.0 NE2 B:HIS320 2.1 13.9 1.0 ND1 B:HIS246 2.1 13.0 1.0 CE1 B:HIS248 2.8 12.3 1.0 NE2 B:HIS263 2.8 26.2 1.0 CE1 B:HIS320 3.0 13.6 1.0 CE1 B:HIS246 3.0 13.4 1.0 S B:SO4401 3.0 22.8 1.0 CD2 B:HIS320 3.1 12.6 1.0 CG B:HIS246 3.1 12.1 1.0 CD2 B:HIS263 3.1 24.0 1.0 CD2 B:HIS248 3.2 10.2 1.0 O3 B:SO4401 3.4 21.7 1.0 CB B:HIS246 3.4 9.9 1.0 O2 B:SO4401 3.6 23.6 1.0 CE1 B:HIS263 3.8 25.9 1.0 ND1 B:HIS248 4.0 10.6 1.0 ND1 B:HIS320 4.1 13.8 1.0 NE2 B:HIS246 4.1 13.7 1.0 CG B:HIS320 4.2 12.7 1.0 CG B:HIS263 4.2 21.5 1.0 O4 B:SO4401 4.2 23.7 1.0 CD2 B:HIS246 4.2 12.9 1.0 CG B:HIS248 4.2 9.3 1.0 ND1 B:HIS263 4.5 24.7 1.0 CG1 B:VAL318 4.8 9.7 1.0 CB B:VAL318 4.9 8.4 1.0 CA B:HIS246 4.9 9.1 1.0

J.S.Elam, A.B.Taylor, R.Strange, S.Antonyuk, P.A.Doucette, J.A.Rodriguez, S.S.Hasnain, L.J.Hayward, J.S.Valentine, T.O.Yeates, P.J.Hart. Amyloid-Like Filaments and Water-Filled Nanotubes Formed By SOD1 Mutant Proteins Linked to Familial Als Nat.Struct.Biol. V. 10 461 2003.
ISSN: ISSN 1072-8368
PubMed: 12754496
DOI: 10.1038/NSB935