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Zinc 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

Other elements in 3sod:

The structure of Changes in Crystallographic Structure and Thermostability of A Cu,Zn Superoxide Dismutase Mutant Resulting From the Removal of Buried Cysteine also contains other interesting chemical elements:

Copper (Cu) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 4 binding sites of Zinc 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 Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3sod

Go back to Zinc Binding Sites List in 3sod
Zinc 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 Zinc with other atoms in the Zn 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:Zn153

b:11.3
occ:1.00
 OD1 O:ASP81 1.8 8.2 1.0
ND1 O:HIS61 1.9 7.5 1.0
ND1 O:HIS78 2.0 3.9 1.0
ND1 O:HIS69 2.1 8.6 1.0
CE1 O:HIS78 2.8 5.2 1.0
CE1 O:HIS61 2.9 8.5 1.0
CG O:ASP81 2.9 10.1 1.0
CG O:HIS61 3.1 7.4 1.0
CE1 O:HIS69 3.1 9.2 1.0
CG O:HIS78 3.1 4.3 1.0
OD2 O:ASP81 3.2 10.3 1.0
CG O:HIS69 3.3 9.2 1.0
CB O:HIS61 3.5 6.4 1.0
CB O:HIS78 3.6 5.1 1.0
CB O:HIS69 3.7 12.1 1.0
NE2 O:HIS78 3.9 4.0 1.0
O O:LYS134 3.9 8.8 1.0
CA O:HIS69 4.0 13.9 1.0
NE2 O:HIS61 4.0 6.4 1.0
CD2 O:HIS61 4.1 6.9 1.0
CD2 O:HIS78 4.1 3.4 1.0
NE2 O:HIS69 4.2 8.0 1.0
CB O:ASP81 4.3 8.3 1.0
CD2 O:HIS69 4.3 9.3 1.0
CA O:ASP81 4.7 8.4 1.0
CA O:HIS78 4.7 9.9 1.0
C O:LYS134 4.7 9.6 1.0
N O:HIS78 4.8 10.9 1.0
N O:ASP81 4.9 8.6 1.0
N O:GLY70 4.9 13.1 1.0
C O:HIS69 4.9 14.2 1.0
CA O:THR135 4.9 9.4 1.0
CD2 O:HIS44 5.0 2.0 1.0
N O:HIS69 5.0 15.0 1.0

Zinc binding site 2 out of 4 in 3sod

Go back to Zinc Binding Sites List in 3sod
Zinc 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 Zinc with other atoms in the Zn 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:Zn153

b:11.3
occ:1.00
 OD1 Y:ASP81 1.8 8.2 1.0
ND1 Y:HIS61 1.9 7.5 1.0
ND1 Y:HIS78 2.0 3.9 1.0
ND1 Y:HIS69 2.1 8.6 1.0
CE1 Y:HIS78 2.8 5.2 1.0
CE1 Y:HIS61 2.9 8.5 1.0
CG Y:ASP81 2.9 10.1 1.0
CG Y:HIS61 3.1 7.4 1.0
CE1 Y:HIS69 3.1 9.2 1.0
CG Y:HIS78 3.1 4.3 1.0
OD2 Y:ASP81 3.2 10.3 1.0
CG Y:HIS69 3.3 9.2 1.0
CB Y:HIS61 3.5 6.4 1.0
CB Y:HIS78 3.6 5.1 1.0
CB Y:HIS69 3.7 12.1 1.0
NE2 Y:HIS78 3.9 4.0 1.0
O Y:LYS134 3.9 8.8 1.0
CA Y:HIS69 4.0 13.9 1.0
NE2 Y:HIS61 4.0 6.4 1.0
CD2 Y:HIS61 4.1 6.9 1.0
CD2 Y:HIS78 4.1 3.4 1.0
NE2 Y:HIS69 4.2 8.0 1.0
CB Y:ASP81 4.3 8.3 1.0
CD2 Y:HIS69 4.3 9.3 1.0
CA Y:ASP81 4.7 8.4 1.0
CA Y:HIS78 4.7 9.9 1.0
C Y:LYS134 4.7 9.6 1.0
N Y:HIS78 4.8 10.9 1.0
N Y:ASP81 4.9 8.6 1.0
N Y:GLY70 4.9 13.1 1.0
C Y:HIS69 4.9 14.2 1.0
CA Y:THR135 4.9 9.4 1.0
CD2 Y:HIS44 5.0 2.0 1.0
N Y:HIS69 5.0 15.0 1.0

Zinc binding site 3 out of 4 in 3sod

Go back to Zinc Binding Sites List in 3sod
Zinc 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 Zinc with other atoms in the Zn 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:Zn153

b:11.3
occ:1.00
 OD1 G:ASP81 1.8 8.2 1.0
ND1 G:HIS61 1.9 7.5 1.0
ND1 G:HIS78 2.0 3.9 1.0
ND1 G:HIS69 2.1 8.6 1.0
CE1 G:HIS78 2.8 5.2 1.0
CE1 G:HIS61 2.9 8.5 1.0
CG G:ASP81 2.9 10.1 1.0
CG G:HIS61 3.1 7.4 1.0
CE1 G:HIS69 3.1 9.2 1.0
CG G:HIS78 3.1 4.3 1.0
OD2 G:ASP81 3.2 10.3 1.0
CG G:HIS69 3.3 9.2 1.0
CB G:HIS61 3.5 6.4 1.0
CB G:HIS78 3.6 5.1 1.0
CB G:HIS69 3.7 12.1 1.0
NE2 G:HIS78 3.9 4.0 1.0
O G:LYS134 3.9 8.8 1.0
CA G:HIS69 4.0 13.9 1.0
NE2 G:HIS61 4.0 6.4 1.0
CD2 G:HIS61 4.1 6.9 1.0
CD2 G:HIS78 4.1 3.4 1.0
NE2 G:HIS69 4.2 8.0 1.0
CB G:ASP81 4.3 8.3 1.0
CD2 G:HIS69 4.3 9.3 1.0
CA G:ASP81 4.7 8.4 1.0
CA G:HIS78 4.7 9.9 1.0
C G:LYS134 4.7 9.6 1.0
N G:HIS78 4.8 10.9 1.0
N G:ASP81 4.9 8.6 1.0
N G:GLY70 4.9 13.1 1.0
C G:HIS69 4.9 14.2 1.0
CA G:THR135 4.9 9.4 1.0
CD2 G:HIS44 5.0 2.0 1.0
N G:HIS69 5.0 15.0 1.0

Zinc binding site 4 out of 4 in 3sod

Go back to Zinc Binding Sites List in 3sod
Zinc 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 Zinc with other atoms in the Zn 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:Zn153

b:11.3
occ:1.00
 OD1 B:ASP81 1.8 8.2 1.0
ND1 B:HIS61 1.9 7.5 1.0
ND1 B:HIS78 2.0 3.9 1.0
ND1 B:HIS69 2.1 8.6 1.0
CE1 B:HIS78 2.8 5.2 1.0
CE1 B:HIS61 2.9 8.5 1.0
CG B:ASP81 2.9 10.1 1.0
CG B:HIS61 3.1 7.4 1.0
CE1 B:HIS69 3.1 9.2 1.0
CG B:HIS78 3.1 4.3 1.0
OD2 B:ASP81 3.2 10.3 1.0
CG B:HIS69 3.3 9.2 1.0
CB B:HIS61 3.5 6.4 1.0
CB B:HIS78 3.6 5.1 1.0
CB B:HIS69 3.7 12.1 1.0
NE2 B:HIS78 3.9 4.0 1.0
O B:LYS134 3.9 8.8 1.0
CA B:HIS69 4.0 13.9 1.0
NE2 B:HIS61 4.0 6.4 1.0
CD2 B:HIS61 4.1 6.9 1.0
CD2 B:HIS78 4.1 3.4 1.0
NE2 B:HIS69 4.2 8.0 1.0
CB B:ASP81 4.3 8.3 1.0
CD2 B:HIS69 4.3 9.3 1.0
CA B:ASP81 4.7 8.4 1.0
CA B:HIS78 4.7 9.9 1.0
C B:LYS134 4.7 9.6 1.0
N B:HIS78 4.8 10.9 1.0
N B:ASP81 4.9 8.6 1.0
N B:GLY70 4.9 13.1 1.0
C B:HIS69 4.9 14.2 1.0
CA B:THR135 4.9 9.4 1.0
CD2 B:HIS44 5.0 2.0 1.0
N B:HIS69 5.0 15.0 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
Page generated: Sat Oct 26 15:57:50 2024

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