Zinc in PDB 8iq0: Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State

Enzymatic activity of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State

All present enzymatic activity of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State, PDB code: 8iq0 was solved by J.H.Zhou, W.X.Huang, R.X.Cheng, P.J.Zhang, Y.C.Zhu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.68 / 1.88
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 74.348, 91.474, 91.164, 85, 78.06, 66.76
R / Rfree (%) 20.1 / 24.5

Other elements in 8iq0:

The structure of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State also contains other interesting chemical elements:

Copper (Cu) 19 atoms
Chlorine (Cl) 2 atoms

Zinc Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State (pdb code 8iq0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 16 binding sites of Zinc where determined in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State, PDB code: 8iq0:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 16 in 8iq0

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Zinc binding site 1 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


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Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:19.5
occ:1.00
OD1 A:ASP81 1.9 19.9 1.0
ND1 A:HIS78 2.0 21.3 1.0
ND1 A:HIS61 2.0 22.4 1.0
ND1 A:HIS69 2.1 22.0 1.0
OD2 A:ASP81 2.4 22.4 1.0
CG A:ASP81 2.5 19.2 1.0
CE1 A:HIS78 2.9 28.8 1.0
CE1 A:HIS69 2.9 22.1 1.0
CE1 A:HIS61 3.0 25.2 1.0
CG A:HIS61 3.0 23.7 1.0
CG A:HIS78 3.2 21.9 1.0
CG A:HIS69 3.3 25.0 1.0
CB A:HIS61 3.4 20.8 1.0
CB A:HIS78 3.6 21.7 1.0
CB A:HIS69 3.8 28.1 1.0
CB A:ASP81 4.0 21.1 1.0
NE2 A:HIS78 4.0 24.1 1.0
O A:LYS134 4.0 29.6 1.0
NE2 A:HIS61 4.1 25.7 1.0
CA A:HIS69 4.1 28.5 1.0
NE2 A:HIS69 4.1 23.5 1.0
CD2 A:HIS61 4.1 23.5 1.0
CD2 A:HIS78 4.2 24.0 1.0
CD2 A:HIS69 4.3 24.3 1.0
CA A:ASP81 4.6 19.3 1.0
CD2 A:HIS44 4.7 22.3 1.0
O A:HOH383 4.7 30.6 1.0
N A:HIS78 4.8 17.3 1.0
N A:GLY70 4.8 26.1 1.0
CA A:HIS78 4.8 17.3 1.0
CA A:HIS61 4.9 20.6 1.0
N A:ASP81 4.9 16.6 1.0
C A:HIS69 5.0 27.2 1.0
NE2 A:HIS44 5.0 24.9 1.0

Zinc binding site 2 out of 16 in 8iq0

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Zinc binding site 2 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


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Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn202

b:25.2
occ:1.00
OD1 B:ASP81 2.0 25.0 1.0
ND1 B:HIS61 2.0 22.8 1.0
ND1 B:HIS69 2.1 25.9 1.0
ND1 B:HIS78 2.1 26.0 1.0
OD2 B:ASP81 2.2 30.1 1.0
CG B:ASP81 2.4 26.8 1.0
CE1 B:HIS69 2.9 24.7 1.0
CE1 B:HIS78 2.9 28.2 1.0
CE1 B:HIS61 3.0 23.3 1.0
CG B:HIS61 3.1 22.0 1.0
CG B:HIS78 3.1 28.1 1.0
CG B:HIS69 3.2 27.2 1.0
CB B:HIS61 3.5 24.1 1.0
CB B:HIS78 3.6 26.9 1.0
CB B:HIS69 3.6 28.2 1.0
O B:LYS134 3.9 32.0 1.0
CB B:ASP81 3.9 25.7 1.0
CA B:HIS69 4.0 31.3 1.0
NE2 B:HIS78 4.0 29.3 1.0
NE2 B:HIS69 4.1 25.7 1.0
NE2 B:HIS61 4.1 22.7 1.0
CD2 B:HIS78 4.1 28.7 1.0
CD2 B:HIS61 4.2 22.5 1.0
CD2 B:HIS69 4.2 27.6 1.0
CA B:ASP81 4.6 22.2 1.0
N B:GLY70 4.7 29.9 1.0
N B:HIS78 4.8 26.4 1.0
CD2 B:HIS44 4.8 23.2 1.0
CA B:HIS78 4.8 27.4 1.0
O B:HOH350 4.8 24.8 1.0
C B:LYS134 4.9 31.9 1.0
N B:ASP81 4.9 20.8 1.0
C B:HIS69 4.9 33.3 1.0
CA B:HIS61 5.0 24.8 1.0

Zinc binding site 3 out of 16 in 8iq0

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Zinc binding site 3 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn202

b:27.6
occ:1.00
ND1 C:HIS78 2.0 28.4 1.0
OD1 C:ASP81 2.0 27.2 1.0
ND1 C:HIS61 2.0 28.9 1.0
ND1 C:HIS69 2.1 32.0 1.0
OD2 C:ASP81 2.3 31.9 1.0
CG C:ASP81 2.5 30.8 1.0
CE1 C:HIS78 2.9 28.7 1.0
CE1 C:HIS69 2.9 32.7 1.0
CG C:HIS78 3.0 28.8 1.0
CE1 C:HIS61 3.0 28.4 1.0
CG C:HIS61 3.0 24.9 1.0
CG C:HIS69 3.2 34.1 1.0
CB C:HIS78 3.4 25.0 1.0
CB C:HIS61 3.4 23.8 1.0
CB C:HIS69 3.7 31.9 1.0
O C:LYS134 3.8 36.5 1.0
NE2 C:HIS78 3.9 31.3 1.0
CB C:ASP81 4.0 30.9 1.0
CA C:HIS69 4.0 34.1 1.0
CD2 C:HIS78 4.0 29.9 1.0
NE2 C:HIS69 4.1 34.5 1.0
NE2 C:HIS61 4.1 27.6 1.0
CD2 C:HIS61 4.2 24.0 1.0
CD2 C:HIS69 4.2 35.5 1.0
N C:HIS78 4.5 26.2 1.0
CA C:HIS78 4.6 24.4 1.0
CA C:ASP81 4.6 28.4 1.0
N C:GLY70 4.7 33.8 1.0
C C:LYS134 4.8 37.7 1.0
N C:ASP81 4.8 23.9 1.0
C C:HIS69 4.9 36.7 1.0
O C:HOH364 4.9 27.4 1.0
CA C:HIS61 4.9 24.9 1.0
N C:HIS69 5.0 35.6 1.0

Zinc binding site 4 out of 16 in 8iq0

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Zinc binding site 4 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn202

b:35.1
occ:1.00
OD1 D:ASP81 1.9 57.2 1.0
OD2 D:ASP81 2.0 61.9 1.0
ND1 D:HIS78 2.0 47.5 1.0
ND1 D:HIS69 2.1 58.8 1.0
ND1 D:HIS61 2.1 38.4 1.0
CG D:ASP81 2.2 56.6 1.0
CG D:HIS78 2.9 44.0 1.0
CE1 D:HIS61 2.9 36.6 1.0
CE1 D:HIS78 2.9 46.1 1.0
CE1 D:HIS69 3.0 58.7 1.0
CG D:HIS69 3.2 62.3 1.0
CG D:HIS61 3.2 33.8 1.0
CB D:HIS78 3.3 41.5 1.0
CB D:HIS69 3.6 77.8 1.0
CB D:HIS61 3.6 31.6 1.0
CB D:ASP81 3.7 46.7 1.0
CA D:HIS69 3.8 43.2 1.0
NE2 D:HIS78 4.0 46.6 1.0
CD2 D:HIS78 4.0 45.6 1.0
NE2 D:HIS61 4.1 35.3 1.0
NE2 D:HIS69 4.1 61.2 1.0
CD2 D:HIS61 4.2 32.8 1.0
CD2 D:HIS69 4.2 63.4 1.0
N D:HIS78 4.3 37.1 1.0
CA D:ASP81 4.4 32.9 1.0
N D:GLY70 4.4 53.1 1.0
CA D:HIS78 4.4 40.0 1.0
C D:HIS69 4.7 52.0 1.0
N D:ASP81 4.7 29.8 1.0
O D:GLY70 4.8 50.2 1.0
N D:HIS69 4.8 44.7 1.0
CD2 D:HIS44 4.9 36.2 1.0

Zinc binding site 5 out of 16 in 8iq0

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Zinc binding site 5 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn202

b:18.0
occ:1.00
OD1 E:ASP81 2.0 17.0 1.0
ND1 E:HIS61 2.0 18.8 1.0
ND1 E:HIS78 2.0 17.5 1.0
ND1 E:HIS69 2.0 19.9 1.0
OD2 E:ASP81 2.3 21.8 1.0
CG E:ASP81 2.5 17.7 1.0
CE1 E:HIS78 2.8 19.6 1.0
CE1 E:HIS69 2.9 15.9 1.0
CE1 E:HIS61 3.0 20.0 1.0
CG E:HIS78 3.1 18.4 1.0
CG E:HIS61 3.1 20.1 1.0
CG E:HIS69 3.2 19.1 1.0
CB E:HIS61 3.4 14.6 1.0
CB E:HIS78 3.6 19.2 1.0
CB E:HIS69 3.6 21.8 1.0
O E:LYS134 3.9 26.3 1.0
NE2 E:HIS78 3.9 20.6 1.0
CB E:ASP81 4.0 16.6 1.0
CA E:HIS69 4.0 22.4 1.0
CD2 E:HIS78 4.0 19.4 1.0
NE2 E:HIS69 4.1 18.8 1.0
NE2 E:HIS61 4.1 19.9 1.0
CD2 E:HIS61 4.2 18.7 1.0
CD2 E:HIS69 4.2 19.5 1.0
CA E:ASP81 4.6 16.4 1.0
N E:HIS78 4.6 17.4 1.0
N E:GLY70 4.7 23.1 1.0
CA E:HIS78 4.7 18.2 1.0
C E:LYS134 4.9 27.0 1.0
CD2 E:HIS44 4.9 19.7 1.0
C E:HIS69 4.9 23.4 1.0
CA E:HIS61 5.0 16.3 1.0
O E:HOH388 5.0 24.6 1.0
N E:ASP81 5.0 14.9 1.0

Zinc binding site 6 out of 16 in 8iq0

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Zinc binding site 6 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn202

b:21.2
occ:1.00
OD1 F:ASP81 1.9 22.6 1.0
ND1 F:HIS78 2.0 21.6 1.0
ND1 F:HIS61 2.0 23.4 1.0
ND1 F:HIS69 2.0 22.4 1.0
OD2 F:ASP81 2.2 26.3 1.0
CG F:ASP81 2.4 23.0 1.0
CE1 F:HIS69 2.9 22.0 1.0
CE1 F:HIS78 2.9 22.7 1.0
CE1 F:HIS61 3.0 23.7 1.0
CG F:HIS61 3.1 21.8 1.0
CG F:HIS78 3.1 24.2 1.0
CG F:HIS69 3.2 24.1 1.0
CB F:HIS61 3.4 21.1 1.0
CB F:HIS78 3.5 20.8 1.0
CB F:HIS69 3.6 24.9 1.0
O F:LYS134 3.9 25.3 1.0
CB F:ASP81 3.9 21.6 1.0
CA F:HIS69 4.0 25.2 1.0
NE2 F:HIS78 4.0 23.5 1.0
NE2 F:HIS69 4.1 23.8 1.0
NE2 F:HIS61 4.1 21.8 1.0
CD2 F:HIS78 4.1 22.9 1.0
CD2 F:HIS61 4.1 21.6 1.0
CD2 F:HIS69 4.2 24.5 1.0
CA F:ASP81 4.6 21.8 1.0
N F:HIS78 4.7 22.8 1.0
N F:GLY70 4.7 25.6 1.0
CA F:HIS78 4.7 21.6 1.0
CD2 F:HIS44 4.9 18.5 1.0
N F:ASP81 4.9 19.3 1.0
C F:HIS69 4.9 27.2 1.0
C F:LYS134 4.9 28.1 1.0
O F:HOH327 5.0 22.7 1.0
CA F:HIS61 5.0 20.2 1.0

Zinc binding site 7 out of 16 in 8iq0

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Zinc binding site 7 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn202

b:22.9
occ:1.00
OD1 G:ASP81 1.9 31.3 1.0
ND1 G:HIS78 2.0 26.1 1.0
ND1 G:HIS69 2.1 28.2 1.0
ND1 G:HIS61 2.1 29.4 1.0
OD2 G:ASP81 2.3 34.2 1.0
CG G:ASP81 2.4 30.4 1.0
CE1 G:HIS78 2.9 26.7 1.0
CE1 G:HIS69 2.9 27.0 1.0
CE1 G:HIS61 3.0 29.2 1.0
CG G:HIS78 3.1 23.8 1.0
CG G:HIS61 3.1 26.8 1.0
CG G:HIS69 3.2 29.2 1.0
CB G:HIS61 3.5 24.5 1.0
CB G:HIS78 3.6 21.1 1.0
CB G:HIS69 3.6 31.2 1.0
O G:LYS134 3.8 28.3 1.0
CB G:ASP81 3.9 25.6 1.0
NE2 G:HIS78 4.0 26.1 1.0
CA G:HIS69 4.0 29.3 1.0
NE2 G:HIS69 4.1 27.8 1.0
CD2 G:HIS78 4.1 25.7 1.0
NE2 G:HIS61 4.1 28.9 1.0
CD2 G:HIS61 4.2 26.9 1.0
CD2 G:HIS69 4.2 28.6 1.0
CA G:ASP81 4.6 21.4 1.0
O G:HOH360 4.7 23.9 1.0
N G:GLY70 4.7 27.6 1.0
N G:HIS78 4.8 21.9 1.0
CA G:HIS78 4.8 20.2 1.0
C G:LYS134 4.9 30.3 1.0
C G:HIS69 4.9 29.5 1.0
N G:ASP81 4.9 16.9 1.0
CA G:HIS61 5.0 21.8 1.0

Zinc binding site 8 out of 16 in 8iq0

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Zinc binding site 8 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn202

b:17.5
occ:1.00
OD1 H:ASP81 2.0 16.9 1.0
ND1 H:HIS61 2.0 17.3 1.0
ND1 H:HIS78 2.0 16.1 1.0
ND1 H:HIS69 2.1 15.7 1.0
OD2 H:ASP81 2.3 19.2 1.0
CG H:ASP81 2.5 16.2 1.0
CE1 H:HIS78 2.9 17.2 1.0
CE1 H:HIS61 2.9 18.0 1.0
CE1 H:HIS69 2.9 15.8 1.0
CG H:HIS61 3.1 17.0 1.0
CG H:HIS78 3.1 18.5 1.0
CG H:HIS69 3.2 17.0 1.0
CB H:HIS61 3.5 17.1 1.0
CB H:HIS78 3.6 15.2 1.0
CB H:HIS69 3.6 18.1 1.0
O H:LYS134 3.8 23.8 1.0
CA H:HIS69 3.9 18.4 1.0
CB H:ASP81 4.0 16.8 1.0
NE2 H:HIS78 4.0 18.1 1.0
NE2 H:HIS61 4.0 18.9 1.0
NE2 H:HIS69 4.1 17.8 1.0
CD2 H:HIS61 4.1 18.0 1.0
CD2 H:HIS78 4.1 17.5 1.0
CD2 H:HIS69 4.2 17.0 1.0
CA H:ASP81 4.6 16.1 1.0
N H:GLY70 4.7 21.4 1.0
N H:HIS78 4.7 17.2 1.0
CA H:HIS78 4.8 17.3 1.0
O H:HOH392 4.8 20.8 1.0
C H:LYS134 4.8 23.9 1.0
C H:HIS69 4.9 18.6 1.0
CD2 H:HIS44 4.9 12.1 1.0
N H:ASP81 4.9 16.4 1.0
N H:HIS69 5.0 19.8 1.0
CA H:HIS61 5.0 17.1 1.0

Zinc binding site 9 out of 16 in 8iq0

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Zinc binding site 9 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn202

b:27.9
occ:1.00
OD1 I:ASP81 2.0 31.4 1.0
ND1 I:HIS78 2.0 30.0 1.0
ND1 I:HIS69 2.0 27.9 1.0
ND1 I:HIS61 2.1 31.8 1.0
OD2 I:ASP81 2.2 34.6 1.0
CG I:ASP81 2.4 31.4 1.0
CE1 I:HIS69 2.8 28.7 1.0
CE1 I:HIS78 2.9 31.8 1.0
CE1 I:HIS61 3.1 32.5 1.0
CG I:HIS78 3.1 29.8 1.0
CG I:HIS61 3.1 31.2 1.0
CG I:HIS69 3.2 30.6 1.0
CB I:HIS61 3.4 27.7 1.0
CB I:HIS78 3.5 28.0 1.0
CB I:HIS69 3.7 33.5 1.0
CB I:ASP81 3.9 28.6 1.0
O I:LYS134 3.9 39.1 1.0
NE2 I:HIS78 4.0 31.5 1.0
NE2 I:HIS69 4.0 29.8 1.0
CA I:HIS69 4.0 34.9 1.0
CD2 I:HIS78 4.1 30.1 1.0
NE2 I:HIS61 4.2 32.6 1.0
CD2 I:HIS69 4.2 30.5 1.0
CD2 I:HIS61 4.2 32.0 1.0
CA I:ASP81 4.6 25.8 1.0
N I:HIS78 4.7 26.8 1.0
O I:HOH349 4.7 33.0 1.0
CA I:HIS78 4.7 27.6 1.0
N I:GLY70 4.8 32.0 1.0
N I:ASP81 4.9 23.6 1.0
CA I:HIS61 5.0 28.1 1.0
C I:LYS134 5.0 40.8 1.0

Zinc binding site 10 out of 16 in 8iq0

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Zinc binding site 10 out of 16 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Oxidized State within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn202

b:33.4
occ:1.00
OD1 J:ASP81 2.0 34.0 1.0
ND1 J:HIS78 2.0 31.2 1.0
ND1 J:HIS69 2.0 35.0 1.0
ND1 J:HIS61 2.1 33.6 1.0
OD2 J:ASP81 2.2 34.3 1.0
CG J:ASP81 2.4 33.0 1.0
CE1 J:HIS78 2.8 32.5 1.0
CE1 J:HIS69 2.9 32.9 1.0
CG J:HIS78 3.0 31.8 1.0
CE1 J:HIS61 3.0 33.2 1.0
CG J:HIS61 3.1 31.9 1.0
CG J:HIS69 3.1 36.2 1.0
CB J:HIS61 3.4 29.2 1.0
CB J:HIS78 3.4 30.5 1.0
CB J:HIS69 3.5 35.4 1.0
CA J:HIS69 3.8 36.1 1.0
CB J:ASP81 3.9 30.9 1.0
NE2 J:HIS78 3.9 32.8 1.0
CD2 J:HIS78 4.0 31.5 1.0
O J:LYS134 4.0 34.7 1.0
NE2 J:HIS69 4.1 35.5 1.0
NE2 J:HIS61 4.2 33.3 1.0
CD2 J:HIS69 4.2 36.5 1.0
CD2 J:HIS61 4.2 31.4 1.0
N J:HIS78 4.6 30.2 1.0
N J:GLY70 4.6 34.3 1.0
CA J:ASP81 4.6 29.8 1.0
CA J:HIS78 4.6 31.5 1.0
C J:HIS69 4.8 37.8 1.0
N J:HIS69 4.8 35.9 1.0
N J:ASP81 4.9 26.9 1.0
CA J:HIS61 4.9 28.5 1.0
C J:LYS134 4.9 38.2 1.0

Reference:

D.D.Wu, S.Jin, R.X.Cheng, W.J.Cai, W.L.Xue, Q.Q.Zhang, L.J.Yang, Q.Zhu, M.Y.Li, G.Lin, Y.Z.Wang, X.P.Mu, Y.Wang, I.Y.Zhang, Q.Zhang, Y.Chen, S.Y.Cai, B.Tan, Y.Li, Y.Q.Chen, P.J.Zhang, C.Sun, Y.Yin, M.J.Wang, Y.Z.Zhu, B.B.Tao, J.H.Zhou, W.X.Huang, Y.C.Zhu. Hydrogen Sulfide Functions As A Micro-Modulator Bound at the Copper Active Site of Cu/Zn-Sod to Regulate the Catalytic Activity of the Enzyme. Cell Rep V. 42 12750 2023.
ISSN: ESSN 2211-1247
PubMed: 37421623
DOI: 10.1016/J.CELREP.2023.112750
Page generated: Thu Oct 31 07:55:03 2024

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