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Copper in PDB 8iq1: Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State

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

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

Protein crystallography data

The structure of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State, PDB code: 8iq1 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) 38.28 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.126, 69.961, 91.345, 98.69, 94.83, 103.31
R / Rfree (%) 18.4 / 21.7

Other elements in 8iq1:

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

Chlorine (Cl) 7 atoms
Zinc (Zn) 8 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State (pdb code 8iq1). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 10 binding sites of Copper where determined in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State, PDB code: 8iq1:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 10 in 8iq1

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Copper binding site 1 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:18.6
occ:1.00
NE2 A:HIS46 1.9 15.1 1.0
ND1 A:HIS44 2.0 19.4 1.0
NE2 A:HIS118 2.1 19.6 1.0
CE1 A:HIS46 2.9 14.8 1.0
CE1 A:HIS44 2.9 16.0 1.0
CD2 A:HIS118 2.9 18.5 1.0
CG A:HIS44 3.0 15.3 1.0
CD2 A:HIS46 3.0 14.2 1.0
CE1 A:HIS118 3.2 18.6 1.0
CB A:HIS44 3.4 14.9 1.0
NE2 A:HIS61 3.5 17.4 1.0
CD2 A:HIS61 3.7 15.9 1.0
CB A:VAL116 3.9 17.6 1.0
O A:HOH372 3.9 27.0 1.0
ND1 A:HIS46 4.0 14.3 1.0
CG1 A:VAL116 4.0 17.2 1.0
NE2 A:HIS44 4.0 15.9 1.0
CD2 A:HIS44 4.1 15.3 1.0
CG A:HIS46 4.1 13.9 1.0
N A:HIS44 4.1 14.9 1.0
CG A:HIS118 4.1 20.8 1.0
ND1 A:HIS118 4.2 20.0 1.0
CA A:HIS44 4.2 14.3 1.0
O A:HOH414 4.3 25.8 1.0
O A:VAL116 4.3 16.4 1.0
O A:HIS44 4.5 14.4 1.0
CE1 A:HIS61 4.5 18.4 1.0
C A:HIS44 4.6 13.9 1.0
CG2 A:VAL116 4.7 17.4 1.0
C A:VAL116 4.8 15.8 1.0
CG A:HIS61 4.8 15.1 1.0
CA A:VAL116 4.9 17.3 1.0

Copper binding site 2 out of 10 in 8iq1

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Copper binding site 2 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:20.6
occ:1.00
NE2 B:HIS46 2.0 16.4 1.0
ND1 B:HIS44 2.0 18.8 1.0
NE2 B:HIS118 2.0 18.8 1.0
CD2 B:HIS118 2.9 18.9 1.0
CE1 B:HIS46 3.0 16.6 1.0
CG B:HIS44 3.0 16.4 1.0
CE1 B:HIS44 3.0 18.0 1.0
CD2 B:HIS46 3.0 13.4 1.0
CE1 B:HIS118 3.1 20.9 1.0
NE2 B:HIS61 3.2 24.3 1.0
CB B:HIS44 3.3 14.4 1.0
CD2 B:HIS61 3.5 24.6 1.0
CB B:VAL116 4.0 13.0 1.0
CG B:HIS118 4.1 19.4 1.0
ND1 B:HIS46 4.1 17.2 1.0
CE1 B:HIS61 4.1 24.8 1.0
CG1 B:VAL116 4.1 16.3 1.0
NE2 B:HIS44 4.1 18.2 1.0
CD2 B:HIS44 4.2 17.1 1.0
ND1 B:HIS118 4.2 20.5 1.0
CG B:HIS46 4.2 15.0 1.0
N B:HIS44 4.2 14.8 1.0
CA B:HIS44 4.3 14.7 1.0
S B:H2S203 4.3 40.8 1.0
O B:VAL116 4.4 16.2 1.0
CG B:HIS61 4.5 22.6 1.0
O B:HIS44 4.6 15.4 1.0
C B:HIS44 4.7 14.5 1.0
ND1 B:HIS61 4.8 22.4 1.0
CG2 B:VAL116 4.9 13.1 1.0
C B:VAL116 4.9 18.4 1.0

Copper binding site 3 out of 10 in 8iq1

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Copper binding site 3 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu201

b:23.6
occ:1.00
NE2 C:HIS46 2.0 18.9 1.0
ND1 C:HIS44 2.1 19.6 1.0
NE2 C:HIS118 2.1 20.3 1.0
CD2 C:HIS118 2.9 17.9 1.0
CG C:HIS44 3.0 18.1 1.0
CD2 C:HIS46 3.0 18.0 1.0
CE1 C:HIS46 3.0 18.2 1.0
CE1 C:HIS44 3.1 20.8 1.0
CB C:HIS44 3.2 16.3 1.0
CE1 C:HIS118 3.2 20.9 1.0
NE2 C:HIS61 3.4 21.8 1.0
CD2 C:HIS61 3.6 19.4 1.0
O C:HOH359 3.8 25.4 1.0
CB C:VAL116 3.9 19.2 1.0
N C:HIS44 4.0 16.0 1.0
CG1 C:VAL116 4.1 20.9 1.0
CA C:HIS44 4.1 15.5 1.0
ND1 C:HIS46 4.1 18.9 1.0
CG C:HIS46 4.1 18.6 1.0
CD2 C:HIS44 4.1 19.9 1.0
CG C:HIS118 4.2 20.1 1.0
NE2 C:HIS44 4.2 20.2 1.0
ND1 C:HIS118 4.2 21.2 1.0
O C:VAL116 4.2 17.1 1.0
O C:HOH395 4.3 32.1 1.0
O C:HIS44 4.3 16.8 1.0
CE1 C:HIS61 4.4 20.6 1.0
C C:HIS44 4.5 17.0 1.0
CG C:HIS61 4.7 20.0 1.0
CG2 C:VAL116 4.7 18.7 1.0
C C:VAL116 4.8 20.1 1.0
CA C:VAL116 4.9 19.2 1.0
C C:PHE43 5.0 21.6 1.0

Copper binding site 4 out of 10 in 8iq1

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Copper binding site 4 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu201

b:17.1
occ:1.00
NE2 D:HIS118 2.0 12.9 1.0
NE2 D:HIS46 2.0 13.3 1.0
ND1 D:HIS44 2.1 12.4 1.0
CE1 D:HIS46 2.8 13.7 1.0
CD2 D:HIS118 2.9 13.2 1.0
CE1 D:HIS118 3.0 13.8 1.0
CE1 D:HIS44 3.1 12.2 1.0
CG D:HIS44 3.1 11.5 1.0
CD2 D:HIS46 3.1 11.9 1.0
NE2 D:HIS61 3.3 17.3 1.0
CB D:HIS44 3.4 11.2 1.0
CD2 D:HIS61 3.5 15.9 1.0
O D:HOH339 3.9 23.5 1.0
CB D:VAL116 3.9 12.4 1.0
ND1 D:HIS46 4.0 13.8 1.0
CG D:HIS118 4.1 14.0 1.0
ND1 D:HIS118 4.1 15.9 1.0
CG1 D:VAL116 4.1 12.9 1.0
CG D:HIS46 4.2 14.7 1.0
NE2 D:HIS44 4.2 11.8 1.0
CD2 D:HIS44 4.2 11.9 1.0
N D:HIS44 4.2 13.4 1.0
CE1 D:HIS61 4.2 15.2 1.0
CL D:CL205 4.3 34.5 1.0
CA D:HIS44 4.3 12.3 1.0
O D:VAL116 4.4 11.8 1.0
CG D:HIS61 4.6 16.0 1.0
O D:HIS44 4.6 11.1 1.0
C D:HIS44 4.8 10.8 1.0
CG2 D:VAL116 4.8 12.4 1.0
C D:VAL116 4.8 13.1 1.0
ND1 D:HIS61 4.9 14.7 1.0
CA D:VAL116 5.0 12.5 1.0

Copper binding site 5 out of 10 in 8iq1

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Copper binding site 5 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu201

b:18.1
occ:1.00
ND1 E:HIS44 2.0 15.7 1.0
NE2 E:HIS46 2.0 14.7 1.0
NE2 E:HIS118 2.1 17.9 1.0
CD2 E:HIS118 2.9 17.8 1.0
CE1 E:HIS46 3.0 15.7 1.0
CG E:HIS44 3.0 14.1 1.0
CE1 E:HIS44 3.0 14.9 1.0
CD2 E:HIS46 3.1 14.4 1.0
CE1 E:HIS118 3.2 18.0 1.0
CB E:HIS44 3.3 13.6 1.0
NE2 E:HIS61 3.5 16.5 1.0
CD2 E:HIS61 3.7 17.2 1.0
O E:HOH361 3.8 20.3 1.0
CB E:VAL116 4.0 14.4 1.0
NE2 E:HIS44 4.1 14.7 1.0
CD2 E:HIS44 4.1 14.2 1.0
ND1 E:HIS46 4.1 14.8 1.0
CG E:HIS118 4.1 18.1 1.0
N E:HIS44 4.2 13.6 1.0
CG E:HIS46 4.2 14.8 1.0
ND1 E:HIS118 4.2 18.0 1.0
CA E:HIS44 4.2 13.1 1.0
CG1 E:VAL116 4.3 15.0 1.0
S E:H2S203 4.3 40.1 1.0
CE1 E:HIS61 4.4 15.3 1.0
O E:VAL116 4.5 14.3 1.0
O E:HIS44 4.5 14.6 1.0
C E:HIS44 4.6 12.9 1.0
CG E:HIS61 4.7 16.5 1.0
CG2 E:VAL116 4.9 17.9 1.0
C E:VAL116 5.0 15.2 1.0

Copper binding site 6 out of 10 in 8iq1

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Copper binding site 6 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu201

b:22.9
occ:1.00
NE2 F:HIS46 2.0 19.7 1.0
ND1 F:HIS44 2.1 20.6 1.0
NE2 F:HIS118 2.1 25.8 1.0
CD2 F:HIS118 3.0 24.9 1.0
CD2 F:HIS46 3.0 19.0 1.0
CE1 F:HIS46 3.0 19.2 1.0
CG F:HIS44 3.1 20.6 1.0
CE1 F:HIS44 3.1 20.6 1.0
CE1 F:HIS118 3.2 25.6 1.0
CB F:HIS44 3.3 19.3 1.0
NE2 F:HIS61 3.4 22.0 1.0
CD2 F:HIS61 3.6 21.2 1.0
O F:HOH345 3.7 27.6 1.0
CB F:VAL116 3.8 19.1 1.0
CG1 F:VAL116 4.0 18.7 1.0
ND1 F:HIS46 4.1 19.1 1.0
CG F:HIS46 4.1 18.6 1.0
CG F:HIS118 4.2 25.8 1.0
N F:HIS44 4.2 15.4 1.0
CD2 F:HIS44 4.2 20.9 1.0
NE2 F:HIS44 4.2 22.1 1.0
CA F:HIS44 4.3 19.3 1.0
ND1 F:HIS118 4.3 24.9 1.0
O F:VAL116 4.3 21.1 1.0
O1 F:EDO203 4.4 27.4 1.0
C1 F:EDO203 4.5 27.8 1.0
CE1 F:HIS61 4.5 21.8 1.0
O F:HIS44 4.5 14.4 1.0
CG2 F:VAL116 4.7 14.7 1.0
C F:HIS44 4.7 14.4 1.0
CG F:HIS61 4.8 20.2 1.0
C F:VAL116 4.8 19.0 1.0
CA F:VAL116 4.9 15.3 1.0

Copper binding site 7 out of 10 in 8iq1

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Copper binding site 7 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cu201

b:19.0
occ:0.55
CU G:CU201 0.0 19.0 0.6
CU G:CU201 0.8 16.6 0.5
ND1 G:HIS44 2.0 19.2 1.0
NE2 G:HIS46 2.1 16.0 1.0
NE2 G:HIS118 2.2 19.8 1.0
NE2 G:HIS61 2.9 20.6 1.0
CE1 G:HIS44 2.9 19.7 1.0
CE1 G:HIS46 3.0 15.7 1.0
CG G:HIS44 3.0 17.5 1.0
CE1 G:HIS118 3.1 21.4 1.0
CD2 G:HIS118 3.2 20.2 1.0
CD2 G:HIS46 3.2 15.6 1.0
CD2 G:HIS61 3.3 19.0 1.0
CB G:HIS44 3.3 15.2 1.0
O G:HOH374 3.4 30.7 1.0
CE1 G:HIS61 3.9 19.7 1.0
NE2 G:HIS44 4.0 20.3 1.0
CD2 G:HIS44 4.1 19.6 1.0
S G:H2S203 4.1 42.0 1.0
ND1 G:HIS46 4.1 16.0 1.0
ND1 G:HIS118 4.2 22.2 1.0
CG G:HIS46 4.3 14.3 1.0
CG G:HIS118 4.3 22.0 1.0
CG G:HIS61 4.3 18.2 1.0
CB G:VAL116 4.4 17.2 1.0
CA G:HIS44 4.4 15.5 1.0
N G:HIS44 4.4 16.1 1.0
CG1 G:VAL116 4.6 16.5 1.0
ND1 G:HIS61 4.6 19.4 1.0
O G:VAL116 4.7 16.8 1.0
O G:HIS44 4.9 15.3 1.0
C G:HIS44 4.9 15.1 1.0

Copper binding site 8 out of 10 in 8iq1

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Copper binding site 8 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cu201

b:16.6
occ:0.46
CU G:CU201 0.0 16.6 0.5
CU G:CU201 0.8 19.0 0.6
NE2 G:HIS118 1.9 19.8 1.0
NE2 G:HIS46 2.0 16.0 1.0
ND1 G:HIS44 2.3 19.2 1.0
CD2 G:HIS118 2.9 20.2 1.0
CE1 G:HIS118 3.0 21.4 1.0
CD2 G:HIS46 3.0 15.6 1.0
CE1 G:HIS46 3.1 15.7 1.0
CG G:HIS44 3.2 17.5 1.0
CE1 G:HIS44 3.3 19.7 1.0
CB G:HIS44 3.4 15.2 1.0
CB G:VAL116 3.6 17.2 1.0
NE2 G:HIS61 3.7 20.6 1.0
CG1 G:VAL116 3.9 16.5 1.0
CD2 G:HIS61 4.0 19.0 1.0
O G:VAL116 4.0 16.8 1.0
O G:HOH374 4.0 30.7 1.0
CG G:HIS118 4.0 22.0 1.0
ND1 G:HIS118 4.1 22.2 1.0
N G:HIS44 4.1 16.1 1.0
ND1 G:HIS46 4.2 16.0 1.0
CG G:HIS46 4.2 14.3 1.0
CA G:HIS44 4.2 15.5 1.0
CD2 G:HIS44 4.4 19.6 1.0
NE2 G:HIS44 4.4 20.3 1.0
O G:HIS44 4.4 15.3 1.0
CG2 G:VAL116 4.5 15.5 1.0
C G:VAL116 4.5 16.9 1.0
S G:H2S203 4.6 42.0 1.0
CA G:VAL116 4.6 16.4 1.0
C G:HIS44 4.7 15.1 1.0
CE1 G:HIS61 4.7 19.7 1.0
C G:PHE43 5.0 16.5 1.0

Copper binding site 9 out of 10 in 8iq1

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Copper binding site 9 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Cu201

b:18.2
occ:0.36
CU H:CU201 0.0 18.2 0.4
CU H:CU201 1.4 18.4 0.6
ND1 H:HIS44 1.8 22.4 1.0
NE2 H:HIS46 2.3 19.6 1.0
CG H:HIS44 2.4 20.4 1.0
NE2 H:HIS61 2.5 24.8 1.0
CB H:HIS44 2.7 16.8 1.0
CD2 H:HIS61 2.8 22.7 1.0
CE1 H:HIS44 2.9 23.9 1.0
NE2 H:HIS118 3.1 23.4 1.0
CD2 H:HIS46 3.2 20.2 1.0
CE1 H:HIS46 3.2 22.5 1.0
CE1 H:HIS61 3.4 22.3 1.0
CD2 H:HIS44 3.6 21.6 1.0
CG H:HIS61 3.7 22.8 1.0
NE2 H:HIS44 3.8 22.4 1.0
CD2 H:HIS118 3.9 21.9 1.0
CA H:HIS44 3.9 16.1 1.0
ND1 H:HIS61 4.0 20.9 1.0
CE1 H:HIS118 4.0 23.1 1.0
N H:HIS44 4.1 19.7 1.0
ND1 H:HIS46 4.2 21.1 1.0
CG H:HIS46 4.2 20.1 1.0
C H:HIS44 4.4 15.9 1.0
O1 H:EDO206 4.5 20.0 1.0
O H:HIS44 4.5 16.0 1.0
CB H:VAL116 4.8 18.8 1.0
CB H:HIS61 4.8 23.3 1.0
O H:VAL116 4.9 16.8 1.0
C H:PHE43 5.0 16.1 1.0
CG H:HIS118 5.0 23.6 1.0

Copper binding site 10 out of 10 in 8iq1

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Copper binding site 10 out of 10 in the Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Crystal Structure of Hydrogen Sulfide-Bound Superoxide Dismutase in Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Cu201

b:18.4
occ:0.64
CU H:CU201 0.0 18.4 0.6
CU H:CU201 1.4 18.2 0.4
NE2 H:HIS118 2.0 23.4 1.0
NE2 H:HIS46 2.0 19.6 1.0
ND1 H:HIS44 2.5 22.4 1.0
CD2 H:HIS118 2.8 21.9 1.0
CE1 H:HIS46 3.0 22.5 1.0
CE1 H:HIS118 3.0 23.1 1.0
CD2 H:HIS46 3.1 20.2 1.0
CG H:HIS44 3.4 20.4 1.0
CE1 H:HIS44 3.5 23.9 1.0
CB H:HIS44 3.6 16.8 1.0
NE2 H:HIS61 3.6 24.8 1.0
CB H:VAL116 3.7 18.8 1.0
CG1 H:VAL116 3.8 20.1 1.0
CD2 H:HIS61 3.9 22.7 1.0
CG H:HIS118 4.0 23.6 1.0
ND1 H:HIS118 4.1 23.5 1.0
O H:VAL116 4.1 16.8 1.0
ND1 H:HIS46 4.1 21.1 1.0
CG H:HIS46 4.2 20.1 1.0
N H:HIS44 4.3 19.7 1.0
CA H:HIS44 4.4 16.1 1.0
O1 H:EDO206 4.5 20.0 1.0
O H:HIS44 4.5 16.0 1.0
CG2 H:VAL116 4.5 19.0 1.0
C H:VAL116 4.6 17.1 1.0
CE1 H:HIS61 4.6 22.3 1.0
CD2 H:HIS44 4.6 21.6 1.0
NE2 H:HIS44 4.6 22.4 1.0
CA H:VAL116 4.7 17.1 1.0
C H:HIS44 4.8 15.9 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 Dec 28 03:52:08 2023

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