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Copper in PDB 2sod: Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase

Enzymatic activity of Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase

All present enzymatic activity of Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase, PDB code: 2sod was solved by J.A.Tainer, E.D.Getzoff, J.S.Richardson, D.C.Richardson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 93.650, 90.330, 71.650, 90.00, 95.10, 90.00
R / Rfree (%) n/a / n/a

Other elements in 2sod:

The structure of Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase (pdb code 2sod). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase, PDB code: 2sod:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2sod

Go back to Copper Binding Sites List in 2sod
Copper binding site 1 out of 4 in the Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu152

b:10.9
occ:1.00
 ND1 O:HIS44 2.0 10.6 1.0
NE2 O:HIS118 2.1 5.9 1.0
NE2 O:HIS46 2.1 10.5 1.0
NE2 O:HIS61 2.2 9.5 1.0
CE1 O:HIS46 2.9 9.6 1.0
CG O:HIS44 2.9 9.9 1.0
CE1 O:HIS118 3.0 5.2 1.0
CE1 O:HIS44 3.0 10.8 1.0
CD2 O:HIS118 3.1 5.0 1.0
CD2 O:HIS61 3.1 10.0 1.0
CB O:HIS44 3.2 10.4 1.0
O O:HOH154 3.2 11.0 1.0
CD2 O:HIS46 3.2 8.1 1.0
CE1 O:HIS61 3.3 9.3 1.0
CG1 O:VAL116 4.0 11.6 1.0
ND1 O:HIS118 4.0 4.1 1.0
CD2 O:HIS44 4.1 9.7 1.0
NE2 O:HIS44 4.1 8.7 1.0
CG O:HIS118 4.1 6.0 1.0
ND1 O:HIS46 4.1 7.8 1.0
CG O:HIS61 4.3 10.6 1.0
CG O:HIS46 4.3 8.0 1.0
ND1 O:HIS61 4.3 10.4 1.0
CA O:HIS44 4.8 11.8 1.0

Copper binding site 2 out of 4 in 2sod

Go back to Copper Binding Sites List in 2sod
Copper binding site 2 out of 4 in the Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
Y:Cu152

b:11.3
occ:1.00
 ND1 Y:HIS44 2.0 9.2 1.0
NE2 Y:HIS61 2.0 9.2 1.0
NE2 Y:HIS118 2.0 9.3 1.0
NE2 Y:HIS46 2.1 11.1 1.0
O Y:HOH154 2.5 11.1 1.0
CE1 Y:HIS118 2.9 7.6 1.0
CE1 Y:HIS61 2.9 9.5 1.0
CG Y:HIS44 3.0 10.3 1.0
CE1 Y:HIS44 3.0 8.5 1.0
CE1 Y:HIS46 3.0 9.4 1.0
CD2 Y:HIS118 3.0 9.2 1.0
CD2 Y:HIS61 3.0 8.8 1.0
CD2 Y:HIS46 3.2 10.1 1.0
CB Y:HIS44 3.3 9.9 1.0
CG1 Y:VAL116 3.8 11.9 1.0
ND1 Y:HIS118 4.0 6.5 1.0
NE2 Y:HIS44 4.0 7.4 1.0
CD2 Y:HIS44 4.1 8.6 1.0
ND1 Y:HIS61 4.1 10.6 1.0
CG Y:HIS118 4.1 9.3 1.0
ND1 Y:HIS46 4.1 9.6 1.0
CG Y:HIS61 4.1 10.6 1.0
CG Y:HIS46 4.3 9.2 1.0
CA Y:HIS44 4.7 11.8 1.0
O Y:THR135 4.8 13.6 1.0
N Y:HIS44 5.0 11.8 1.0
O Y:HIS44 5.0 11.8 1.0

Copper binding site 3 out of 4 in 2sod

Go back to Copper Binding Sites List in 2sod
Copper binding site 3 out of 4 in the Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu152

b:11.2
occ:1.00
 NE2 B:HIS118 2.0 7.2 1.0
ND1 B:HIS44 2.0 10.2 1.0
NE2 B:HIS46 2.1 6.2 1.0
NE2 B:HIS61 2.3 8.3 1.0
CE1 B:HIS44 2.9 8.7 1.0
CE1 B:HIS118 2.9 6.2 1.0
CD2 B:HIS118 3.0 7.8 1.0
CE1 B:HIS46 3.0 5.8 1.0
CG B:HIS44 3.0 10.3 1.0
CD2 B:HIS61 3.1 7.4 1.0
CD2 B:HIS46 3.2 5.5 1.0
CE1 B:HIS61 3.3 7.2 1.0
CB B:HIS44 3.5 10.4 1.0
O B:HOH154 3.9 8.5 1.0
CG1 B:VAL116 4.0 10.8 1.0
ND1 B:HIS118 4.0 7.0 1.0
NE2 B:HIS44 4.0 8.8 1.0
CG B:HIS118 4.1 7.7 1.0
CD2 B:HIS44 4.1 9.0 1.0
ND1 B:HIS46 4.2 5.1 1.0
CG B:HIS61 4.2 9.3 1.0
ND1 B:HIS61 4.3 9.1 1.0
CG B:HIS46 4.3 6.6 1.0
CA B:HIS44 4.6 11.9 1.0
N B:HIS44 4.6 11.8 1.0
CB B:VAL116 4.8 10.2 1.0
C B:HIS44 4.9 11.9 1.0
O B:HIS44 5.0 11.7 1.0

Copper binding site 4 out of 4 in 2sod

Go back to Copper Binding Sites List in 2sod
Copper binding site 4 out of 4 in the Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Determination and Analysis of the 2 Angstrom Structure of Copper, Zinc Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cu152

b:11.7
occ:1.00
 NE2 G:HIS46 2.0 8.8 1.0
ND1 G:HIS44 2.1 9.5 1.0
NE2 G:HIS118 2.1 9.4 1.0
NE2 G:HIS61 2.2 9.6 1.0
CG G:HIS44 2.9 9.2 1.0
CE1 G:HIS46 2.9 8.2 1.0
CD2 G:HIS61 3.0 10.0 1.0
CE1 G:HIS44 3.0 9.0 1.0
CD2 G:HIS46 3.0 9.0 1.0
CE1 G:HIS118 3.0 8.7 1.0
CD2 G:HIS118 3.1 9.2 1.0
CB G:HIS44 3.2 10.4 1.0
CE1 G:HIS61 3.3 9.1 1.0
O G:HOH154 3.8 16.0 1.0
CD2 G:HIS44 3.9 8.5 1.0
NE2 G:HIS44 3.9 8.8 1.0
ND1 G:HIS46 4.0 8.2 1.0
CG G:HIS46 4.1 8.5 1.0
ND1 G:HIS118 4.1 7.2 1.0
CG G:HIS118 4.2 9.1 1.0
CG G:HIS61 4.2 10.1 1.0
ND1 G:HIS61 4.3 9.0 1.0
CA G:HIS44 4.5 11.8 1.0
CG1 G:VAL116 4.6 8.3 1.0
N G:HIS44 4.7 11.8 1.0
CG2 G:VAL116 4.8 8.9 1.0
C G:HIS44 5.0 11.9 1.0

Reference:

J.A.Tainer, E.D.Getzoff, K.M.Beem, J.S.Richardson, D.C.Richardson. Determination and Analysis of the 2 A-Structure of Copper, Zinc Superoxide Dismutase. J.Mol.Biol. V. 160 181 1982.
ISSN: ISSN 0022-2836
PubMed: 7175933
DOI: 10.1016/0022-2836(82)90174-7
Page generated: Wed Jul 31 00:01:49 2024

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