Zinc in PDB 2wz5: L38V SOD1 Mutant Complexed with L-Methionine.

All present enzymatic activity of L38V SOD1 Mutant Complexed with L-Methionine.:
1.15.1.1;

The structure of L38V SOD1 Mutant Complexed with L-Methionine., PDB code: 2wz5 was solved by S.V.Antonyuk, R.W.Strange, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.00 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.996, 68.025, 50.633, 90.00, 105.88, 90.00
R / Rfree (%)	19.2 / 25.5

The structure of L38V SOD1 Mutant Complexed with L-Methionine. also contains other interesting chemical elements:

Copper

(Cu)

3 atoms

The binding sites of Zinc atom in the L38V SOD1 Mutant Complexed with L-Methionine. (pdb code 2wz5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the L38V SOD1 Mutant Complexed with L-Methionine., PDB code: 2wz5:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the L38V SOD1 Mutant Complexed with L-Methionine.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L38V SOD1 Mutant Complexed with L-Methionine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn154 b:18.5 occ:0.20 CU A:CU154 1.2 17.2 0.8 NE2 A:HIS120 1.9 16.4 1.0 NE2 A:HIS48 2.2 14.7 1.0 CE1 A:HIS120 2.5 15.4 1.0 ND1 A:HIS46 2.6 15.9 1.0 CE1 A:HIS48 2.8 14.0 1.0 NE2 A:HIS63 2.9 17.0 1.0 O A:HOH2166 2.9 25.8 1.0 O A:HOH2186 3.0 25.5 0.5 CD2 A:HIS120 3.1 14.1 1.0 CE1 A:HIS46 3.3 18.0 1.0 CD2 A:HIS63 3.4 15.5 1.0 CD2 A:HIS48 3.5 13.8 1.0 CG A:HIS46 3.7 14.2 1.0 ND1 A:HIS120 3.7 12.2 1.0 CE1 A:HIS63 3.9 13.4 1.0 CG A:HIS120 4.0 12.6 1.0 ND1 A:HIS48 4.0 13.1 1.0 CB A:HIS46 4.1 12.5 1.0 CG A:HIS48 4.4 11.9 1.0 O A:HOH2195 4.4 16.9 0.7 NE2 A:HIS46 4.5 15.3 1.0 CG A:HIS63 4.5 14.3 1.0 CG1 A:VAL118 4.6 12.3 1.0 O A:HOH2088 4.7 28.6 1.0 CD2 A:HIS46 4.7 14.5 1.0 CB A:VAL118 4.7 10.4 1.0 ND1 A:HIS63 4.8 15.1 1.0

Zinc binding site 2 out of 3 in the L38V SOD1 Mutant Complexed with L-Methionine.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of L38V SOD1 Mutant Complexed with L-Methionine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn155 b:13.7 occ:1.00 OD1 A:ASP83 1.9 11.3 1.0 ND1 A:HIS80 2.0 12.6 1.0 ND1 A:HIS63 2.0 15.1 1.0 ND1 A:HIS71 2.1 13.0 1.0 CG A:ASP83 2.7 14.6 1.0 OD2 A:ASP83 2.8 12.5 1.0 CE1 A:HIS71 2.9 13.3 1.0 CE1 A:HIS63 2.9 13.4 1.0 CE1 A:HIS80 2.9 11.6 1.0 CG A:HIS80 3.1 12.4 1.0 CG A:HIS63 3.1 14.3 1.0 CG A:HIS71 3.2 13.9 1.0 CB A:HIS63 3.5 13.9 1.0 CB A:HIS80 3.5 12.9 1.0 CB A:HIS71 3.7 14.8 1.0 CA A:HIS71 4.0 14.6 1.0 O A:LYS136 4.0 20.2 1.0 NE2 A:HIS80 4.1 14.8 1.0 NE2 A:HIS71 4.1 11.5 1.0 NE2 A:HIS63 4.1 17.0 1.0 CD2 A:HIS80 4.1 14.2 1.0 CB A:ASP83 4.2 14.1 1.0 CD2 A:HIS63 4.2 15.5 1.0 CD2 A:HIS71 4.2 13.9 1.0 CA A:ASP83 4.7 12.3 1.0 N A:HIS80 4.7 12.4 1.0 CA A:HIS80 4.7 13.0 1.0 N A:GLY72 4.8 14.3 1.0 O A:HOH2164 4.9 22.7 1.0 N A:ASP83 4.9 12.1 1.0 C A:HIS71 4.9 14.2 1.0 N A:HIS71 5.0 15.7 1.0 CA A:HIS63 5.0 13.2 1.0

Zinc binding site 3 out of 3 in the L38V SOD1 Mutant Complexed with L-Methionine.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of L38V SOD1 Mutant Complexed with L-Methionine. within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn155 b:12.1 occ:1.00 OD1 F:ASP83 2.0 12.4 1.0 ND1 F:HIS63 2.0 12.4 1.0 ND1 F:HIS80 2.0 11.6 1.0 ND1 F:HIS71 2.0 10.6 1.0 CG F:ASP83 2.7 12.3 1.0 OD2 F:ASP83 2.8 12.2 1.0 CE1 F:HIS71 2.9 11.9 1.0 CE1 F:HIS80 2.9 11.7 1.0 CE1 F:HIS63 2.9 13.4 1.0 CG F:HIS63 3.1 12.6 1.0 CG F:HIS80 3.1 13.4 1.0 CG F:HIS71 3.1 12.8 1.0 CB F:HIS63 3.5 12.6 1.0 CB F:HIS80 3.6 11.8 1.0 CB F:HIS71 3.6 13.1 1.0 O F:LYS136 3.9 17.2 1.0 CA F:HIS71 3.9 13.8 1.0 NE2 F:HIS80 4.0 12.1 1.0 NE2 F:HIS63 4.1 16.2 1.0 NE2 F:HIS71 4.1 11.2 1.0 CD2 F:HIS80 4.1 13.3 1.0 CD2 F:HIS63 4.1 13.5 1.0 CB F:ASP83 4.2 12.9 1.0 CD2 F:HIS71 4.2 12.5 1.0 N F:HIS80 4.7 12.0 1.0 CA F:ASP83 4.7 11.7 1.0 N F:GLY72 4.8 12.5 1.0 CA F:HIS80 4.8 12.0 1.0 C F:LYS136 4.9 17.9 1.0 N F:HIS71 4.9 14.3 1.0 C F:HIS71 4.9 13.8 1.0 O F:HOH2183 4.9 10.9 0.5 N F:ASP83 4.9 10.6 1.0 CA F:HIS63 5.0 11.6 1.0

S.Antonyuk, R.W.Strange, S.S.Hasnain. Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights For Lead Optimization. J.Med.Chem. V. 53 1402 2010.
ISSN: ISSN 0022-2623
PubMed: 20067275
DOI: 10.1021/JM9017948