Zinc in PDB 7wx1: E40K/M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris)

Enzymatic activity of E40K/M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris)

All present enzymatic activity of E40K/M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris):
1.15.1.1;

Protein crystallography data

The structure of E40K/M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris), PDB code: 7wx1 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) 46.48 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.511, 50.17, 185.751, 90, 90, 90
R / Rfree (%) 23.1 / 26.2

Other elements in 7wx1:

The structure of E40K/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 E40K/M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris) (pdb code 7wx1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the E40K/M117L Variant of Cu/Zn-Superoxide Dismutase From Dog (Canis Familiaris), PDB code: 7wx1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7wx1

Go back to Zinc Binding Sites List in 7wx1
Zinc binding site 1 out of 2 in the E40K/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 E40K/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:33.5
occ:1.00
ND1 A:HIS80 1.8 28.0 1.0
OD1 A:ASP83 1.8 40.5 1.0
ND1 A:HIS63 2.1 38.6 1.0
ND1 A:HIS71 2.2 26.3 1.0
CG A:ASP83 2.5 35.6 1.0
OD2 A:ASP83 2.6 36.0 1.0
CE1 A:HIS80 2.7 28.9 1.0
CG A:HIS80 2.9 29.9 1.0
CG A:HIS63 3.1 39.1 1.0
CE1 A:HIS71 3.1 32.5 1.0
CE1 A:HIS63 3.2 41.1 1.0
CG A:HIS71 3.2 28.6 1.0
CB A:HIS63 3.3 38.4 1.0
CB A:HIS80 3.4 31.0 1.0
CB A:HIS71 3.5 31.6 1.0
O A:GLN136 3.6 36.6 1.0
CA A:HIS71 3.8 31.4 1.0
NE2 A:HIS80 3.8 30.3 1.0
CD2 A:HIS80 3.9 30.6 1.0
CB A:ASP83 4.0 36.1 1.0
CD2 A:HIS63 4.2 39.5 1.0
NE2 A:HIS63 4.3 37.5 1.0
NE2 A:HIS71 4.3 33.0 1.0
CD2 A:HIS71 4.3 27.4 1.0
N A:HIS80 4.6 33.9 1.0
CA A:HIS80 4.6 33.7 1.0
CA A:ASP83 4.6 37.4 1.0
C A:GLN136 4.6 35.0 1.0
N A:GLY72 4.7 35.1 1.0
N A:HIS71 4.8 30.5 1.0
C A:HIS71 4.8 32.8 1.0
O A:HOH340 4.8 34.1 1.0
CA A:HIS63 4.9 37.0 1.0
N A:ASP83 4.9 35.7 1.0

Zinc binding site 2 out of 2 in 7wx1

Go back to Zinc Binding Sites List in 7wx1
Zinc binding site 2 out of 2 in the E40K/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 E40K/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:29.4
occ:1.00
ND1 B:HIS80 2.0 30.4 1.0
ND1 B:HIS63 2.0 29.4 1.0
OD1 B:ASP83 2.0 24.9 1.0
ND1 B:HIS71 2.1 32.3 1.0
CG B:ASP83 2.7 29.0 1.0
OD2 B:ASP83 2.8 30.2 1.0
CE1 B:HIS80 2.9 28.6 1.0
CE1 B:HIS63 3.0 32.1 1.0
CG B:HIS63 3.0 30.5 1.0
CE1 B:HIS71 3.1 29.9 1.0
CG B:HIS80 3.1 28.7 1.0
CG B:HIS71 3.2 32.6 1.0
CB B:HIS63 3.4 32.9 1.0
CB B:HIS71 3.5 31.5 1.0
CB B:HIS80 3.5 29.7 1.0
O B:GLN136 3.8 32.3 1.0
CA B:HIS71 3.8 30.4 1.0
NE2 B:HIS80 4.0 29.1 1.0
NE2 B:HIS63 4.1 33.5 1.0
CD2 B:HIS80 4.1 27.6 1.0
CD2 B:HIS63 4.1 31.4 1.0
CB B:ASP83 4.2 29.5 1.0
NE2 B:HIS71 4.2 30.5 1.0
CD2 B:HIS71 4.3 30.9 1.0
N B:HIS80 4.7 31.3 1.0
CA B:HIS80 4.7 30.3 1.0
CA B:ASP83 4.7 28.3 1.0
C B:GLN136 4.7 34.9 1.0
N B:GLY72 4.7 30.2 1.0
O B:HOH321 4.8 28.3 1.0
C B:HIS71 4.9 31.3 1.0
CD2 B:HIS46 4.9 31.9 1.0
N B:HIS71 4.9 34.5 1.0
CA B:HIS63 4.9 31.9 1.0
N B:ASP83 5.0 29.7 1.0

Reference:

S.Narikiyo, Y.Furukawa, M.Akutsu. Crystal Structure of Dog Superoxide Dismutase To Be Published.
Page generated: Sat Apr 8 05:34:26 2023

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