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Zinc in PDB 2wko: Structure of Metal Loaded Pathogenic SOD1 Mutant G93A.

Enzymatic activity of Structure of Metal Loaded Pathogenic SOD1 Mutant G93A.

All present enzymatic activity of Structure of Metal Loaded Pathogenic SOD1 Mutant G93A.:
1.15.1.1;

Protein crystallography data

The structure of Structure of Metal Loaded Pathogenic SOD1 Mutant G93A., PDB code: 2wko was solved by S.V.Antonyuk, A.Galaleldeen, R.Strange, L.Whitson, N.Narayana, A.Taylor, J.P.Schuermann, S.P.Holloway, S.S.Hasnain, P.J.Hart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 56.80 / 1.97
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.488, 47.157, 56.356, 90.00, 90.38, 90.00
R / Rfree (%) 17.36 / 23.072

Other elements in 2wko:

The structure of Structure of Metal Loaded Pathogenic SOD1 Mutant G93A. also contains other interesting chemical elements:

Iodine (I) 4 atoms
Copper (Cu) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Metal Loaded Pathogenic SOD1 Mutant G93A. (pdb code 2wko). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Metal Loaded Pathogenic SOD1 Mutant G93A., PDB code: 2wko:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2wko

Go back to Zinc Binding Sites List in 2wko
Zinc binding site 1 out of 2 in the Structure of Metal Loaded Pathogenic SOD1 Mutant G93A.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Metal Loaded Pathogenic SOD1 Mutant G93A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn155

b:27.4
occ:1.00
OD1 A:ASP83 1.9 21.0 1.0
ND1 A:HIS63 2.0 23.3 1.0
ND1 A:HIS80 2.0 23.4 1.0
ND1 A:HIS71 2.2 28.4 1.0
CG A:ASP83 2.8 21.9 1.0
CE1 A:HIS80 2.8 24.1 1.0
OD2 A:ASP83 2.9 22.1 1.0
CE1 A:HIS63 3.0 19.5 1.0
CG A:HIS63 3.0 21.2 1.0
CG A:HIS80 3.1 23.1 1.0
CE1 A:HIS71 3.1 29.9 1.0
CG A:HIS71 3.3 28.1 1.0
CB A:HIS63 3.3 21.0 1.0
CB A:HIS80 3.6 26.4 1.0
CB A:HIS71 3.7 28.2 1.0
CA A:HIS71 4.0 28.3 1.0
NE2 A:HIS80 4.0 25.1 1.0
O A:LYS136 4.1 26.8 1.0
NE2 A:HIS63 4.1 21.0 1.0
CD2 A:HIS63 4.1 23.4 1.0
CD2 A:HIS80 4.1 23.1 1.0
CB A:ASP83 4.2 22.4 1.0
NE2 A:HIS71 4.3 27.9 1.0
CD2 A:HIS71 4.4 26.7 1.0
CA A:ASP83 4.7 23.2 1.0
N A:HIS80 4.8 28.0 1.0
CA A:HIS80 4.8 26.5 1.0
N A:GLY72 4.8 27.1 1.0
CA A:HIS63 4.9 21.7 1.0
CD2 A:HIS46 4.9 21.6 1.0
N A:ASP83 4.9 23.0 1.0
N A:HIS71 4.9 28.9 1.0
C A:HIS71 4.9 28.2 1.0
O A:HOH2119 5.0 26.4 1.0

Zinc binding site 2 out of 2 in 2wko

Go back to Zinc Binding Sites List in 2wko
Zinc binding site 2 out of 2 in the Structure of Metal Loaded Pathogenic SOD1 Mutant G93A.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Metal Loaded Pathogenic SOD1 Mutant G93A. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn155

b:22.2
occ:1.00
ND1 F:HIS63 2.0 15.1 1.0
OD1 F:ASP83 2.0 16.4 1.0
ND1 F:HIS71 2.0 14.4 1.0
ND1 F:HIS80 2.1 20.7 1.0
OD2 F:ASP83 2.8 17.5 1.0
CG F:ASP83 2.8 18.8 1.0
CE1 F:HIS71 2.9 18.5 1.0
CE1 F:HIS80 2.9 22.0 1.0
CE1 F:HIS63 3.0 16.1 1.0
CG F:HIS63 3.1 17.8 1.0
CG F:HIS80 3.1 19.3 1.0
CG F:HIS71 3.1 16.2 1.0
CB F:HIS63 3.4 18.7 1.0
CB F:HIS80 3.6 18.0 1.0
CB F:HIS71 3.6 18.4 1.0
CA F:HIS71 3.9 19.1 1.0
NE2 F:HIS80 4.1 17.2 1.0
NE2 F:HIS71 4.1 19.2 1.0
O F:LYS136 4.1 23.2 1.0
NE2 F:HIS63 4.1 17.7 1.0
CD2 F:HIS80 4.2 16.9 1.0
CD2 F:HIS63 4.2 18.6 1.0
CD2 F:HIS71 4.2 15.3 1.0
CB F:ASP83 4.2 18.5 1.0
N F:HIS80 4.7 18.1 1.0
CA F:ASP83 4.7 18.4 1.0
CA F:HIS80 4.8 17.8 1.0
N F:GLY72 4.8 20.4 1.0
CD2 F:HIS46 4.8 15.2 1.0
C F:HIS71 4.9 20.1 1.0
CA F:HIS63 4.9 19.6 1.0
O F:HOH2144 5.0 24.0 1.0
C F:LYS136 5.0 22.4 1.0
N F:HIS71 5.0 20.3 1.0

Reference:

A.Galaleldeen, R.W.Strange, L.J.Whitson, S.V.Antonyuk, N.Narayana, A.B.Taylor, J.P.Schuermann, S.P.Holloway, S.S.Hasnain, P.J.Hart. Structural and Biophysical Properties of Metal- Free Pathogenic SOD1 Mutants A4V and G93A. Arch.Biochem.Biophys. V. 492 40 2009.
ISSN: ISSN 0003-9861
PubMed: 19800308
DOI: 10.1016/J.ABB.2009.09.020
Page generated: Wed Dec 16 03:58:06 2020

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