Zinc in PDB 7wwy: M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris)

Enzymatic activity of M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris)

All present enzymatic activity of M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris):
1.15.1.1;

Protein crystallography data

The structure of M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris), PDB code: 7wwy was solved by S.Narikiyo, Y.Furukawa, M.Akutsu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.71 / 1.50
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 50.643, 50.643, 282.12, 90, 90, 90
R / Rfree (%) 25.6 / 28.7

Other elements in 7wwy:

The structure of M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris) also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris) (pdb code 7wwy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris), PDB code: 7wwy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7wwy

Go back to Zinc Binding Sites List in 7wwy
Zinc binding site 1 out of 2 in the M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:17.5
occ:1.00
OD1 A:ASP83 2.0 17.4 1.0
ND1 A:HIS80 2.0 16.2 1.0
ND1 A:HIS63 2.0 15.4 1.0
ND1 A:HIS71 2.1 17.2 1.0
CG A:ASP83 2.8 16.0 1.0
CE1 A:HIS71 2.9 14.1 1.0
OD2 A:ASP83 2.9 17.0 1.0
CE1 A:HIS80 2.9 14.7 1.0
CE1 A:HIS63 3.0 18.7 1.0
CG A:HIS63 3.0 16.5 1.0
CG A:HIS80 3.1 18.1 1.0
CG A:HIS71 3.2 15.1 1.0
CB A:HIS63 3.4 16.1 1.0
CB A:HIS80 3.6 18.2 1.0
CB A:HIS71 3.6 16.7 1.0
O A:GLN136 3.8 16.6 1.0
CA A:HIS71 3.9 16.1 1.0
NE2 A:HIS71 4.1 14.7 1.0
NE2 A:HIS80 4.1 18.2 1.0
NE2 A:HIS63 4.1 20.4 1.0
CD2 A:HIS63 4.2 19.2 1.0
CB A:ASP83 4.2 16.2 1.0
CD2 A:HIS80 4.2 15.6 1.0
CD2 A:HIS71 4.2 14.7 1.0
N A:HIS80 4.7 18.1 1.0
CA A:ASP83 4.7 16.8 1.0
C A:GLN136 4.7 17.6 1.0
N A:GLY72 4.8 15.7 1.0
CA A:HIS80 4.8 17.4 1.0
O A:HOH401 4.8 19.8 1.0
CD2 A:HIS46 4.9 19.1 1.0
CA A:HIS63 4.9 15.9 1.0
N A:HIS71 4.9 16.1 1.0
C A:HIS71 4.9 17.1 1.0
N A:ASP83 5.0 15.5 1.0

Zinc binding site 2 out of 2 in 7wwy

Go back to Zinc Binding Sites List in 7wwy
Zinc binding site 2 out of 2 in the M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:35.0
occ:1.00
ND1 B:HIS63 1.8 33.4 1.0
ND1 B:HIS80 2.0 30.7 1.0
OD1 B:ASP83 2.0 33.2 1.0
ND1 B:HIS71 2.1 35.4 1.0
CE1 B:HIS63 2.8 33.4 1.0
CG B:HIS63 2.9 34.7 1.0
CG B:ASP83 2.9 39.1 1.0
CE1 B:HIS80 2.9 35.4 1.0
CE1 B:HIS71 2.9 38.9 1.0
CG B:HIS80 3.0 31.4 1.0
OD2 B:ASP83 3.2 36.3 1.0
CG B:HIS71 3.2 40.9 1.0
CB B:HIS63 3.3 39.4 1.0
CB B:HIS80 3.4 35.4 1.0
CB B:HIS71 3.6 35.8 1.0
O B:GLN136 3.8 41.5 1.0
CA B:HIS71 3.9 36.9 1.0
NE2 B:HIS63 4.0 32.3 1.0
NE2 B:HIS80 4.0 34.0 1.0
CD2 B:HIS63 4.0 32.8 1.0
CD2 B:HIS80 4.0 32.0 1.0
NE2 B:HIS71 4.1 38.5 1.0
CD2 B:HIS71 4.2 41.0 1.0
CB B:ASP83 4.3 37.4 1.0
O B:HOH351 4.6 41.2 1.0
CD2 B:HIS46 4.7 33.3 1.0
N B:GLY72 4.7 40.6 1.0
CA B:HIS80 4.7 35.5 1.0
N B:HIS80 4.7 34.9 1.0
CA B:ASP83 4.7 33.3 1.0
C B:HIS71 4.8 43.8 1.0
CA B:HIS63 4.8 38.3 1.0
C B:GLN136 4.9 44.0 1.0
N B:HIS71 4.9 35.8 1.0
O B:GLY72 5.0 41.0 1.0
N B:ASP83 5.0 35.4 1.0

Reference:

S.Narikiyo, Y.Furukawa, M.Akutsu. Crystal Structure of Dog Superoxide Dismutase To Be Published.
Page generated: Sat Apr 8 05:31:10 2023

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