Atomistry » Copper » PDB 1oe2-1rjp » 1pu0
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1pu0 »

Copper in PDB 1pu0: Structure of Human Cu,Zn Superoxide Dismutase

Enzymatic activity of Structure of Human Cu,Zn Superoxide Dismutase

All present enzymatic activity of Structure of Human Cu,Zn Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Structure of Human Cu,Zn Superoxide Dismutase, PDB code: 1pu0 was solved by M.Didonato, L.Craig, M.E.Huff, M.M.Thayer, R.M.F.Cardoso, C.J.Kassmann, T.P.Lo, C.K.Bruns, E.T.Powers, J.W.Kelly, E.D.Getzoff, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 203.580, 165.680, 144.150, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 24.3

Other elements in 1pu0:

The structure of Structure of Human Cu,Zn Superoxide Dismutase also contains other interesting chemical elements:

Zinc (Zn) 10 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Human Cu,Zn Superoxide Dismutase (pdb code 1pu0). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 10 binding sites of Copper where determined in the Structure of Human Cu,Zn Superoxide Dismutase, PDB code: 1pu0:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 1 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu200

b:24.4
occ:1.00
NE2 A:HIS48 2.0 21.0 1.0
NE2 A:HIS120 2.1 20.3 1.0
ND1 A:HIS46 2.1 25.5 1.0
CD2 A:HIS120 2.9 29.7 1.0
CE1 A:HIS48 2.9 24.3 1.0
CE1 A:HIS46 3.1 28.6 1.0
CG A:HIS46 3.1 28.2 1.0
CD2 A:HIS48 3.1 18.6 1.0
CE1 A:HIS120 3.2 24.7 1.0
NE2 A:HIS63 3.3 34.3 1.0
CB A:HIS46 3.5 23.0 1.0
CD2 A:HIS63 3.6 32.1 1.0
CB A:VAL118 3.9 22.8 1.0
ND1 A:HIS48 4.1 22.3 1.0
CG A:HIS120 4.1 27.8 1.0
CG A:HIS48 4.2 23.4 1.0
NE2 A:HIS46 4.2 24.3 1.0
CG1 A:VAL118 4.2 22.4 1.0
ND1 A:HIS120 4.2 23.2 1.0
CD2 A:HIS46 4.2 23.7 1.0
N A:HIS46 4.2 23.0 1.0
CE1 A:HIS63 4.3 27.6 1.0
CA A:HIS46 4.3 22.3 1.0
O A:HOH400 4.4 34.9 1.0
O A:VAL118 4.6 21.3 1.0
O A:HIS46 4.6 20.6 1.0
CG2 A:VAL118 4.6 20.7 1.0
CG A:HIS63 4.7 29.1 1.0
C A:HIS46 4.7 28.6 1.0
C A:VAL118 5.0 23.0 1.0

Copper binding site 2 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 2 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu200

b:21.1
occ:1.00
NE2 B:HIS48 2.0 20.0 1.0
ND1 B:HIS46 2.0 20.3 1.0
NE2 B:HIS120 2.0 23.9 1.0
CE1 B:HIS48 2.9 21.1 1.0
CD2 B:HIS120 3.0 25.8 1.0
CG B:HIS46 3.0 22.5 1.0
CE1 B:HIS46 3.0 21.5 1.0
CD2 B:HIS48 3.1 20.1 1.0
CE1 B:HIS120 3.1 20.4 1.0
NE2 B:HIS63 3.3 21.7 1.0
CB B:HIS46 3.3 20.7 1.0
CD2 B:HIS63 3.6 25.5 1.0
O B:HOH430 3.7 39.6 1.0
CB B:VAL118 4.0 20.2 1.0
O B:HOH401 4.0 31.4 1.0
ND1 B:HIS48 4.0 24.1 1.0
CG B:HIS120 4.1 18.0 1.0
CG1 B:VAL118 4.1 17.7 1.0
CD2 B:HIS46 4.1 23.0 1.0
ND1 B:HIS120 4.2 17.7 1.0
NE2 B:HIS46 4.2 19.6 1.0
CG B:HIS48 4.2 21.3 1.0
N B:HIS46 4.2 17.8 1.0
CE1 B:HIS63 4.3 21.8 1.0
CA B:HIS46 4.3 18.8 1.0
O B:VAL118 4.5 18.0 1.0
O B:HIS46 4.5 18.8 1.0
CG2 B:VAL118 4.7 20.4 1.0
C B:HIS46 4.7 19.1 1.0
CG B:HIS63 4.7 17.8 1.0
C B:VAL118 5.0 19.9 1.0
ND1 B:HIS63 5.0 19.2 1.0

Copper binding site 3 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 3 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu200

b:40.6
occ:1.00
NE2 C:HIS120 2.0 31.0 1.0
NE2 C:HIS48 2.0 23.4 1.0
ND1 C:HIS46 2.0 51.2 1.0
CD2 C:HIS120 2.9 27.4 1.0
CE1 C:HIS48 2.9 24.1 1.0
CD2 C:HIS48 3.0 30.8 1.0
CE1 C:HIS46 3.0 56.3 1.0
CE1 C:HIS120 3.0 36.8 1.0
CG C:HIS46 3.0 45.8 1.0
CB C:HIS46 3.4 26.2 1.0
NE2 C:HIS63 3.5 50.6 1.0
CD2 C:HIS63 3.9 46.2 1.0
CB C:VAL118 4.0 29.0 1.0
CG C:HIS120 4.0 33.2 1.0
ND1 C:HIS48 4.0 29.3 1.0
CE1 C:HIS63 4.1 51.8 1.0
ND1 C:HIS120 4.1 30.6 1.0
CG C:HIS48 4.1 27.1 1.0
NE2 C:HIS46 4.1 45.6 1.0
CD2 C:HIS46 4.1 46.0 1.0
CG1 C:VAL118 4.2 35.8 1.0
O C:HOH402 4.2 44.0 1.0
N C:HIS46 4.3 36.1 1.0
CA C:HIS46 4.4 26.4 1.0
CG2 C:VAL118 4.6 28.6 1.0
O C:VAL118 4.7 34.1 1.0
CG C:HIS63 4.7 44.7 1.0
ND1 C:HIS63 4.7 45.6 1.0
O C:HIS46 4.8 32.5 1.0
C C:HIS46 4.8 37.6 1.0

Copper binding site 4 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 4 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu200

b:22.9
occ:1.00
NE2 D:HIS48 2.0 24.5 1.0
NE2 D:HIS120 2.0 19.9 1.0
ND1 D:HIS46 2.0 21.1 1.0
CD2 D:HIS120 2.9 19.4 1.0
CE1 D:HIS48 3.0 25.2 1.0
CE1 D:HIS46 3.0 22.2 1.0
CD2 D:HIS48 3.0 23.1 1.0
CG D:HIS46 3.0 23.3 1.0
CE1 D:HIS120 3.0 21.4 1.0
CB D:HIS46 3.4 17.9 1.0
NE2 D:HIS63 3.4 27.0 1.0
O D:HOH403 3.7 29.8 1.0
CD2 D:HIS63 3.8 24.0 1.0
CB D:VAL118 3.9 19.0 1.0
CG1 D:VAL118 4.1 20.8 1.0
ND1 D:HIS48 4.1 20.0 1.0
CG D:HIS120 4.1 19.8 1.0
NE2 D:HIS46 4.1 21.9 1.0
ND1 D:HIS120 4.1 18.4 1.0
CG D:HIS48 4.1 21.1 1.0
CD2 D:HIS46 4.1 22.6 1.0
N D:HIS46 4.2 18.9 1.0
CA D:HIS46 4.3 17.3 1.0
CE1 D:HIS63 4.3 19.6 1.0
O D:VAL118 4.5 20.8 1.0
O D:HIS46 4.5 20.7 1.0
C D:HIS46 4.6 21.9 1.0
CG2 D:VAL118 4.7 22.1 1.0
CG D:HIS63 4.8 23.7 1.0
C D:VAL118 5.0 22.3 1.0

Copper binding site 5 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 5 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu200

b:22.5
occ:1.00
NE2 E:HIS48 2.0 20.8 1.0
ND1 E:HIS46 2.0 19.8 1.0
NE2 E:HIS120 2.0 21.2 1.0
CD2 E:HIS120 2.9 19.3 1.0
CD2 E:HIS48 3.0 23.4 1.0
CG E:HIS46 3.0 19.3 1.0
CE1 E:HIS48 3.0 20.6 1.0
CE1 E:HIS46 3.0 21.4 1.0
CE1 E:HIS120 3.1 27.1 1.0
CB E:HIS46 3.3 20.9 1.0
NE2 E:HIS63 3.3 25.6 1.0
CD2 E:HIS63 3.7 23.7 1.0
O E:HOH1129 3.8 30.9 1.0
CB E:VAL118 3.9 20.3 1.0
ND1 E:HIS48 4.1 22.5 1.0
CG E:HIS48 4.1 20.5 1.0
NE2 E:HIS46 4.1 25.3 1.0
CG E:HIS120 4.1 19.9 1.0
CD2 E:HIS46 4.1 24.6 1.0
ND1 E:HIS120 4.1 21.3 1.0
CG1 E:VAL118 4.1 22.3 1.0
N E:HIS46 4.2 19.6 1.0
CE1 E:HIS63 4.2 26.2 1.0
CA E:HIS46 4.2 22.1 1.0
O E:HIS46 4.5 20.2 1.0
O E:VAL118 4.5 20.0 1.0
C E:HIS46 4.6 23.0 1.0
CG2 E:VAL118 4.7 20.7 1.0
CG E:HIS63 4.7 25.0 1.0
ND1 E:HIS63 5.0 25.7 1.0
C E:VAL118 5.0 22.8 1.0

Copper binding site 6 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 6 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu200

b:21.4
occ:1.00
NE2 F:HIS48 2.0 16.6 1.0
NE2 F:HIS120 2.0 19.5 1.0
ND1 F:HIS46 2.1 22.4 1.0
CD2 F:HIS120 2.9 17.5 1.0
CE1 F:HIS48 2.9 19.7 1.0
CD2 F:HIS48 3.0 19.3 1.0
CG F:HIS46 3.0 18.1 1.0
CE1 F:HIS120 3.0 18.4 1.0
CE1 F:HIS46 3.1 22.2 1.0
CB F:HIS46 3.3 20.8 1.0
NE2 F:HIS63 3.4 24.6 1.0
O F:HOH404 3.7 28.3 1.0
CD2 F:HIS63 3.8 24.9 1.0
CB F:VAL118 3.9 19.6 1.0
ND1 F:HIS48 4.0 18.9 1.0
CG F:HIS120 4.1 17.0 1.0
ND1 F:HIS120 4.1 17.9 1.0
CG F:HIS48 4.1 19.1 1.0
CG1 F:VAL118 4.1 23.2 1.0
CD2 F:HIS46 4.2 18.5 1.0
NE2 F:HIS46 4.2 21.4 1.0
N F:HIS46 4.2 16.1 1.0
CE1 F:HIS63 4.2 21.2 1.0
CA F:HIS46 4.3 16.2 1.0
O F:VAL118 4.5 18.5 1.0
O F:HIS46 4.6 19.5 1.0
CG2 F:VAL118 4.7 21.0 1.0
C F:HIS46 4.7 23.6 1.0
CG F:HIS63 4.8 19.4 1.0
C F:VAL118 5.0 21.5 1.0

Copper binding site 7 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 7 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cu200

b:35.6
occ:1.00
ND1 G:HIS46 1.9 41.6 1.0
NE2 G:HIS120 2.0 30.9 1.0
NE2 G:HIS48 2.1 35.7 1.0
CD2 G:HIS120 2.9 31.2 1.0
CG G:HIS46 2.9 42.8 1.0
CE1 G:HIS46 3.0 44.0 1.0
CE1 G:HIS120 3.0 37.9 1.0
CE1 G:HIS48 3.1 30.4 1.0
CD2 G:HIS48 3.1 29.6 1.0
CB G:HIS46 3.3 33.6 1.0
NE2 G:HIS63 3.5 40.0 1.0
O G:HOH1467 3.5 48.2 1.0
CD2 G:HIS63 3.7 33.8 1.0
CB G:VAL118 4.0 26.9 1.0
CG G:HIS120 4.1 28.4 1.0
NE2 G:HIS46 4.1 39.6 1.0
ND1 G:HIS120 4.1 36.6 1.0
CD2 G:HIS46 4.1 37.6 1.0
CG1 G:VAL118 4.1 29.5 1.0
N G:HIS46 4.1 30.4 1.0
O G:HOH405 4.1 40.4 1.0
ND1 G:HIS48 4.2 31.2 1.0
CA G:HIS46 4.2 29.0 1.0
CG G:HIS48 4.2 22.9 1.0
CE1 G:HIS63 4.4 42.9 1.0
O G:VAL118 4.4 28.2 1.0
O G:HIS46 4.5 27.8 1.0
C G:HIS46 4.6 43.8 1.0
CG G:HIS63 4.7 38.0 1.0
CG2 G:VAL118 4.7 35.5 1.0
C G:VAL118 4.9 30.9 1.0
C G:PHE45 5.0 42.3 1.0
CA G:VAL118 5.0 22.1 1.0

Copper binding site 8 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 8 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Cu200

b:25.9
occ:1.00
ND1 H:HIS46 2.0 23.1 1.0
NE2 H:HIS48 2.0 23.9 1.0
NE2 H:HIS120 2.0 21.7 1.0
CE1 H:HIS46 2.9 25.8 1.0
CD2 H:HIS120 3.0 21.8 1.0
CE1 H:HIS48 3.0 28.5 1.0
CD2 H:HIS48 3.0 24.4 1.0
CE1 H:HIS120 3.0 23.0 1.0
CG H:HIS46 3.0 23.9 1.0
NE2 H:HIS63 3.3 29.1 1.0
CB H:HIS46 3.4 24.6 1.0
CD2 H:HIS63 3.7 27.9 1.0
CB H:VAL118 4.0 25.2 1.0
NE2 H:HIS46 4.1 25.0 1.0
ND1 H:HIS120 4.1 23.5 1.0
ND1 H:HIS48 4.1 24.4 1.0
CG H:HIS120 4.1 26.1 1.0
CD2 H:HIS46 4.1 22.8 1.0
CG1 H:VAL118 4.1 22.8 1.0
CG H:HIS48 4.2 20.9 1.0
O H:HOH406 4.2 42.8 1.0
N H:HIS46 4.2 20.9 1.0
CE1 H:HIS63 4.2 29.9 1.0
CA H:HIS46 4.3 23.1 1.0
O H:VAL118 4.5 24.9 1.0
O H:HIS46 4.5 23.4 1.0
C H:HIS46 4.7 26.3 1.0
CG H:HIS63 4.7 29.2 1.0
CG2 H:VAL118 4.7 29.1 1.0
C H:VAL118 5.0 24.0 1.0
ND1 H:HIS63 5.0 28.7 1.0

Copper binding site 9 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 9 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Cu200

b:35.8
occ:1.00
NE2 I:HIS120 2.0 31.9 1.0
ND1 I:HIS46 2.0 32.0 1.0
NE2 I:HIS48 2.0 35.7 1.0
CD2 I:HIS120 2.9 30.7 1.0
CG I:HIS46 2.9 33.6 1.0
CE1 I:HIS48 2.9 32.0 1.0
CE1 I:HIS46 3.0 29.9 1.0
CE1 I:HIS120 3.0 31.5 1.0
CD2 I:HIS48 3.1 31.9 1.0
CB I:HIS46 3.3 26.8 1.0
NE2 I:HIS63 3.5 34.5 1.0
CD2 I:HIS63 3.8 33.0 1.0
CB I:VAL118 4.0 31.3 1.0
CG I:HIS120 4.1 30.8 1.0
CD2 I:HIS46 4.1 31.7 1.0
NE2 I:HIS46 4.1 26.3 1.0
ND1 I:HIS48 4.1 32.8 1.0
ND1 I:HIS120 4.1 36.9 1.0
N I:HIS46 4.1 28.1 1.0
CG I:HIS48 4.2 33.7 1.0
CA I:HIS46 4.2 28.5 1.0
CG1 I:VAL118 4.3 23.4 1.0
CE1 I:HIS63 4.3 33.5 1.0
O I:VAL118 4.5 27.5 1.0
O I:HIS46 4.5 27.3 1.0
CG2 I:VAL118 4.6 30.8 1.0
C I:HIS46 4.7 30.4 1.0
CG I:HIS63 4.8 36.2 1.0
C I:VAL118 5.0 24.2 1.0

Copper binding site 10 out of 10 in 1pu0

Go back to Copper Binding Sites List in 1pu0
Copper binding site 10 out of 10 in the Structure of Human Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Cu200

b:24.9
occ:1.00
NE2 J:HIS48 2.0 24.5 1.0
NE2 J:HIS120 2.1 22.6 1.0
ND1 J:HIS46 2.1 23.0 1.0
CD2 J:HIS48 2.9 23.5 1.0
CE1 J:HIS48 3.0 27.5 1.0
CD2 J:HIS120 3.0 22.0 1.0
CE1 J:HIS46 3.1 29.5 1.0
CG J:HIS46 3.1 26.1 1.0
CE1 J:HIS120 3.1 24.4 1.0
NE2 J:HIS63 3.2 29.1 1.0
CB J:HIS46 3.4 20.7 1.0
CD2 J:HIS63 3.6 27.0 1.0
O J:HOH429 3.7 49.6 1.0
O J:HOH408 3.8 39.3 1.0
CB J:VAL118 4.0 23.8 1.0
CG1 J:VAL118 4.0 27.3 1.0
ND1 J:HIS48 4.1 26.7 1.0
CG J:HIS48 4.1 24.2 1.0
ND1 J:HIS120 4.2 19.7 1.0
CG J:HIS120 4.2 19.2 1.0
NE2 J:HIS46 4.2 23.2 1.0
CD2 J:HIS46 4.2 21.0 1.0
N J:HIS46 4.2 20.1 1.0
CE1 J:HIS63 4.2 26.4 1.0
CA J:HIS46 4.3 21.1 1.0
O J:HIS46 4.5 22.7 1.0
O J:VAL118 4.5 22.3 1.0
CG J:HIS63 4.7 26.2 1.0
C J:HIS46 4.7 20.9 1.0
CG2 J:VAL118 4.8 23.3 1.0

Reference:

M.Didonato, L.Craig, M.E.Huff, M.M.Thayer, R.M.F.Cardoso, C.J.Kassmann, T.P.Lo, C.K.Bruns, E.T.Powers, J.W.Kelly, E.D.Getzoff, J.A.Tainer. Als Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization J.Mol.Biol. V. 332 601 2003.
ISSN: ISSN 0022-2836
PubMed: 12963370
DOI: 10.1016/S0022-2836(03)00889-1
Page generated: Sun Dec 13 11:01:28 2020

Last articles

Zn in 7NA9
Zn in 7LZP
Zn in 7M1H
Zn in 7L6V
Zn in 7CM0
V in 7P8R
Ni in 7L19
Na in 7T88
Na in 7MJ5
Na in 7L00
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy