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Copper in PDB 3sod: Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine

Enzymatic activity of Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine

All present enzymatic activity of Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine:
1.15.1.1;

Protein crystallography data

The structure of Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine, PDB code: 3sod was solved by D.E.Mcree, S.M.Redford, E.D.Getzoff, J.R.Lepock, R.A.Hallewell, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 92.500, 89.400, 70.500, 90.00, 95.70, 90.00
R / Rfree (%) 19 / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine (pdb code 3sod). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine, PDB code: 3sod:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 3sod

Go back to Copper Binding Sites List in 3sod
Copper binding site 1 out of 4 in the Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu152

b:16.8
occ:1.00
NE2 O:HIS118 2.0 7.0 1.0
ND1 O:HIS44 2.0 2.0 1.0
NE2 O:HIS46 2.1 4.8 1.0
NE2 O:HIS61 2.2 6.4 1.0
CD2 O:HIS118 2.9 6.8 1.0
CE1 O:HIS118 2.9 7.0 1.0
CE1 O:HIS46 3.0 4.3 1.0
CG O:HIS44 3.0 2.0 1.0
CE1 O:HIS44 3.1 2.6 1.0
CD2 O:HIS61 3.2 6.9 1.0
CD2 O:HIS46 3.2 4.9 1.0
CE1 O:HIS61 3.2 8.5 1.0
CB O:HIS44 3.3 2.3 1.0
ND1 O:HIS118 3.9 6.6 1.0
CG O:HIS118 4.0 6.4 1.0
NE2 O:HIS44 4.1 2.7 1.0
CG2 O:VAL116 4.2 4.4 1.0
ND1 O:HIS46 4.2 3.4 1.0
CD2 O:HIS44 4.2 2.0 1.0
CG O:HIS46 4.3 4.3 1.0
CG O:HIS61 4.3 7.4 1.0
ND1 O:HIS61 4.4 7.5 1.0
CA O:HIS44 4.6 2.4 1.0
N O:HIS44 4.6 2.8 1.0

Copper binding site 2 out of 4 in 3sod

Go back to Copper Binding Sites List in 3sod
Copper binding site 2 out of 4 in the Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
Y:Cu152

b:16.8
occ:1.00
NE2 Y:HIS118 2.0 7.0 1.0
ND1 Y:HIS44 2.0 2.0 1.0
NE2 Y:HIS46 2.1 4.8 1.0
NE2 Y:HIS61 2.2 6.4 1.0
CD2 Y:HIS118 2.9 6.8 1.0
CE1 Y:HIS118 2.9 7.0 1.0
CE1 Y:HIS46 3.0 4.3 1.0
CG Y:HIS44 3.0 2.0 1.0
CE1 Y:HIS44 3.1 2.6 1.0
CD2 Y:HIS61 3.2 6.9 1.0
CD2 Y:HIS46 3.2 4.9 1.0
CE1 Y:HIS61 3.2 8.5 1.0
CB Y:HIS44 3.3 2.3 1.0
ND1 Y:HIS118 3.9 6.6 1.0
CG Y:HIS118 4.0 6.4 1.0
NE2 Y:HIS44 4.1 2.7 1.0
CG2 Y:VAL116 4.2 4.4 1.0
ND1 Y:HIS46 4.2 3.4 1.0
CD2 Y:HIS44 4.2 2.0 1.0
CG Y:HIS46 4.3 4.3 1.0
CG Y:HIS61 4.3 7.4 1.0
ND1 Y:HIS61 4.4 7.5 1.0
CA Y:HIS44 4.6 2.4 1.0
N Y:HIS44 4.6 2.8 1.0

Copper binding site 3 out of 4 in 3sod

Go back to Copper Binding Sites List in 3sod
Copper binding site 3 out of 4 in the Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cu152

b:16.8
occ:1.00
NE2 G:HIS118 2.0 7.0 1.0
ND1 G:HIS44 2.0 2.0 1.0
NE2 G:HIS46 2.1 4.8 1.0
NE2 G:HIS61 2.2 6.4 1.0
CD2 G:HIS118 2.9 6.8 1.0
CE1 G:HIS118 2.9 7.0 1.0
CE1 G:HIS46 3.0 4.3 1.0
CG G:HIS44 3.0 2.0 1.0
CE1 G:HIS44 3.1 2.6 1.0
CD2 G:HIS61 3.2 6.9 1.0
CD2 G:HIS46 3.2 4.9 1.0
CE1 G:HIS61 3.2 8.5 1.0
CB G:HIS44 3.3 2.3 1.0
ND1 G:HIS118 3.9 6.6 1.0
CG G:HIS118 4.0 6.4 1.0
NE2 G:HIS44 4.1 2.7 1.0
CG2 G:VAL116 4.2 4.4 1.0
ND1 G:HIS46 4.2 3.4 1.0
CD2 G:HIS44 4.2 2.0 1.0
CG G:HIS46 4.3 4.3 1.0
CG G:HIS61 4.3 7.4 1.0
ND1 G:HIS61 4.4 7.5 1.0
CA G:HIS44 4.6 2.4 1.0
N G:HIS44 4.6 2.8 1.0

Copper binding site 4 out of 4 in 3sod

Go back to Copper Binding Sites List in 3sod
Copper binding site 4 out of 4 in the Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu152

b:16.8
occ:1.00
NE2 B:HIS118 2.0 7.0 1.0
ND1 B:HIS44 2.0 2.0 1.0
NE2 B:HIS46 2.1 4.8 1.0
NE2 B:HIS61 2.2 6.4 1.0
CD2 B:HIS118 2.9 6.8 1.0
CE1 B:HIS118 2.9 7.0 1.0
CE1 B:HIS46 3.0 4.3 1.0
CG B:HIS44 3.0 2.0 1.0
CE1 B:HIS44 3.1 2.6 1.0
CD2 B:HIS61 3.2 6.9 1.0
CD2 B:HIS46 3.2 4.9 1.0
CE1 B:HIS61 3.2 8.5 1.0
CB B:HIS44 3.3 2.3 1.0
ND1 B:HIS118 3.9 6.6 1.0
CG B:HIS118 4.0 6.4 1.0
NE2 B:HIS44 4.1 2.7 1.0
CG2 B:VAL116 4.2 4.4 1.0
ND1 B:HIS46 4.2 3.4 1.0
CD2 B:HIS44 4.2 2.0 1.0
CG B:HIS46 4.3 4.3 1.0
CG B:HIS61 4.3 7.4 1.0
ND1 B:HIS61 4.4 7.5 1.0
CA B:HIS44 4.6 2.4 1.0
N B:HIS44 4.6 2.8 1.0

Reference:

D.E.Mcree, S.M.Redford, E.D.Getzoff, J.R.Lepock, R.A.Hallewell, J.A.Tainer. Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of A Buried Cysteine. J.Biol.Chem. V. 265 14234 1990.
ISSN: ISSN 0021-9258
PubMed: 2387847
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