Atomistry » Copper » PDB 1mg2-1oe1 » 1pu0
Atomistry »
  Copper »
    PDB 1mg2-1oe1 »
      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

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: Thu Sep 3 16:14:28 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy