Copper 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:

Zinc

(Zn)

3 atoms

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

Copper 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 Copper with other atoms in the Cu binding site number 1 of L38V SOD1 Mutant Complexed with L-Methionine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu154 b:17.2 occ:0.80 ZN A:ZN154A 1.2 18.5 0.2 NE2 A:HIS48 2.0 14.7 1.0 ND1 A:HIS46 2.1 15.9 1.0 NE2 A:HIS120 2.1 16.4 1.0 CD2 A:HIS48 2.9 13.8 1.0 CG A:HIS46 2.9 14.2 1.0 CD2 A:HIS120 3.0 14.1 1.0 CE1 A:HIS48 3.0 14.0 1.0 CE1 A:HIS46 3.1 18.0 1.0 CB A:HIS46 3.2 12.5 1.0 CE1 A:HIS120 3.2 15.4 1.0 NE2 A:HIS63 3.5 17.0 1.0 CD2 A:HIS63 3.8 15.5 1.0 O A:HOH2166 3.9 25.8 1.0 CB A:VAL118 4.0 10.4 1.0 CG A:HIS48 4.1 11.9 1.0 ND1 A:HIS48 4.1 13.1 1.0 CD2 A:HIS46 4.1 14.5 1.0 CG A:HIS120 4.1 12.6 1.0 CG1 A:VAL118 4.2 12.3 1.0 CA A:HIS46 4.2 11.0 1.0 NE2 A:HIS46 4.2 15.3 1.0 O A:HOH2186 4.2 25.5 0.5 ND1 A:HIS120 4.2 12.2 1.0 N A:HIS46 4.2 9.6 1.0 CE1 A:HIS63 4.3 13.4 1.0 O A:HIS46 4.5 10.4 1.0 O A:VAL118 4.5 13.0 1.0 C A:HIS46 4.6 10.5 1.0 CG A:HIS63 4.7 14.3 1.0 CG2 A:VAL118 4.7 11.2 1.0 ND1 A:HIS63 5.0 15.1 1.0

Copper 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 Copper with other atoms in the Cu binding site number 2 of L38V SOD1 Mutant Complexed with L-Methionine. within 5.0Å range: probe atom residue distance (Å) B Occ F:Cu154 b:13.8 occ:0.70 CU F:CU154 0.0 13.8 0.7 CU F:CU154 1.1 22.2 0.3 NE2 F:HIS48 2.0 13.6 1.0 ND1 F:HIS46 2.1 14.4 1.0 NE2 F:HIS120 2.1 15.2 1.0 CD2 F:HIS120 2.9 13.9 1.0 CD2 F:HIS48 3.0 12.4 1.0 CG F:HIS46 3.0 13.6 1.0 CE1 F:HIS48 3.0 12.6 1.0 CE1 F:HIS46 3.1 15.1 1.0 CE1 F:HIS120 3.2 14.2 1.0 CB F:HIS46 3.2 11.8 1.0 NE2 F:HIS63 3.4 16.2 1.0 CD2 F:HIS63 3.7 13.5 1.0 O F:HOH2185 3.8 24.7 1.0 CB F:VAL118 4.0 10.5 1.0 O F:HOH2192 4.0 26.4 1.0 CG F:HIS120 4.1 11.8 1.0 CG F:HIS48 4.1 11.6 1.0 ND1 F:HIS48 4.1 13.0 1.0 CA F:HIS46 4.1 9.8 1.0 CD2 F:HIS46 4.2 13.4 1.0 CG1 F:VAL118 4.2 11.9 1.0 N F:HIS46 4.2 8.4 1.0 NE2 F:HIS46 4.2 15.4 1.0 ND1 F:HIS120 4.2 12.1 1.0 CE1 F:HIS63 4.3 13.4 1.0 O F:HIS46 4.5 9.9 1.0 O F:VAL118 4.6 11.1 1.0 C F:HIS46 4.6 9.4 1.0 CG2 F:VAL118 4.6 10.5 1.0 CG F:HIS63 4.8 12.6 1.0

Copper 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 Copper with other atoms in the Cu binding site number 3 of L38V SOD1 Mutant Complexed with L-Methionine. within 5.0Å range: probe atom residue distance (Å) B Occ F:Cu154 b:22.2 occ:0.30 CU F:CU154 0.0 22.2 0.3 CU F:CU154 1.1 13.8 0.7 NE2 F:HIS120 1.9 15.2 1.0 NE2 F:HIS48 2.3 13.6 1.0 ND1 F:HIS46 2.4 14.4 1.0 CE1 F:HIS120 2.6 14.2 1.0 NE2 F:HIS63 2.8 16.2 1.0 O F:HOH2185 2.8 24.7 1.0 CE1 F:HIS48 2.9 12.6 1.0 O F:HOH2192 3.0 26.4 1.0 CD2 F:HIS120 3.0 13.9 1.0 CE1 F:HIS46 3.1 15.1 1.0 CD2 F:HIS63 3.3 13.5 1.0 CD2 F:HIS48 3.5 12.4 1.0 CG F:HIS46 3.5 13.6 1.0 ND1 F:HIS120 3.8 12.1 1.0 CE1 F:HIS63 3.8 13.4 1.0 CG F:HIS120 4.0 11.8 1.0 CB F:HIS46 4.0 11.8 1.0 ND1 F:HIS48 4.1 13.0 1.0 NE2 F:HIS46 4.3 15.4 1.0 CG F:HIS48 4.5 11.6 1.0 CG F:HIS63 4.5 12.6 1.0 CD2 F:HIS46 4.5 13.4 1.0 O A:HOH2192 4.6 20.7 1.0 O F:HOH2084 4.7 25.4 1.0 CG1 F:VAL118 4.7 11.9 1.0 ND1 F:HIS63 4.7 12.4 1.0 CB F:VAL118 4.8 10.5 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