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Zinc in PDB 2aeo: Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase

Enzymatic activity of Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase

All present enzymatic activity of Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase, PDB code: 2aeo was solved by V.Calderone, A.Casini, S.Mangani, L.Messori, P.L.Orioli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.90 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.207, 50.920, 146.738, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.6

Other elements in 2aeo:

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

Platinum (Pt) 2 atoms
Copper (Cu) 2 atoms
Chlorine (Cl) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase (pdb code 2aeo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase, PDB code: 2aeo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2aeo

Go back to Zinc Binding Sites List in 2aeo
Zinc binding site 1 out of 2 in the Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn153

b:5.8
occ:1.00
ND1 A:HIS61 2.0 3.6 1.0
OD1 A:ASP81 2.0 7.2 1.0
ND1 A:HIS78 2.0 4.7 1.0
ND1 A:HIS69 2.1 2.0 1.0
CE1 A:HIS78 2.8 5.1 1.0
CG A:ASP81 2.8 3.7 1.0
CE1 A:HIS61 2.9 5.2 1.0
OD2 A:ASP81 2.9 3.4 1.0
CE1 A:HIS69 3.0 3.0 1.0
CG A:HIS61 3.1 4.6 1.0
CG A:HIS78 3.2 4.1 1.0
CG A:HIS69 3.2 2.9 1.0
CB A:HIS61 3.5 3.9 1.0
CB A:HIS69 3.6 2.8 1.0
O A:LYS134 3.6 4.5 1.0
CB A:HIS78 3.7 3.3 1.0
NE2 A:HIS78 4.0 2.9 1.0
CA A:HIS69 4.0 4.1 1.0
NE2 A:HIS61 4.0 6.2 1.0
CD2 A:HIS61 4.1 4.1 1.0
CD2 A:HIS78 4.1 4.3 1.0
NE2 A:HIS69 4.2 2.0 1.0
CB A:ASP81 4.3 2.4 1.0
CD2 A:HIS69 4.3 2.0 1.0
O A:HOH326 4.5 5.4 1.0
C A:LYS134 4.6 4.9 1.0
CA A:ASP81 4.8 2.9 1.0
N A:HIS78 4.8 3.2 1.0
N A:GLY70 4.8 3.4 1.0
CA A:HIS78 4.9 3.2 1.0
N A:HIS69 5.0 4.4 1.0
CA A:THR135 5.0 3.4 1.0
CA A:HIS61 5.0 3.5 1.0
C A:HIS69 5.0 4.8 1.0

Zinc binding site 2 out of 2 in 2aeo

Go back to Zinc Binding Sites List in 2aeo
Zinc binding site 2 out of 2 in the Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn153

b:8.1
occ:1.00
ND1 B:HIS61 1.9 7.9 1.0
OD1 B:ASP81 2.0 7.3 1.0
ND1 B:HIS78 2.1 3.3 1.0
ND1 B:HIS69 2.2 5.6 1.0
CE1 B:HIS61 2.8 8.0 1.0
CG B:ASP81 2.8 2.0 1.0
CE1 B:HIS78 2.9 3.2 1.0
CG B:HIS61 3.0 5.9 1.0
OD2 B:ASP81 3.0 3.8 1.0
CE1 B:HIS69 3.2 6.3 1.0
CG B:HIS78 3.2 3.9 1.0
CG B:HIS69 3.2 5.6 1.0
CB B:HIS61 3.4 5.2 1.0
CB B:HIS69 3.5 4.8 1.0
CB B:HIS78 3.6 2.8 1.0
O B:LYS134 3.7 6.3 1.0
CA B:HIS69 3.9 5.5 1.0
NE2 B:HIS61 3.9 6.9 1.0
CD2 B:HIS61 4.0 6.2 1.0
NE2 B:HIS78 4.1 2.0 1.0
CD2 B:HIS78 4.2 3.1 1.0
CB B:ASP81 4.3 4.6 1.0
NE2 B:HIS69 4.3 4.9 1.0
CD2 B:HIS69 4.3 4.4 1.0
O B:HOH297 4.5 2.0 1.0
C B:LYS134 4.7 6.8 1.0
CA B:ASP81 4.8 4.1 1.0
N B:HIS78 4.8 3.4 1.0
CA B:HIS78 4.8 3.6 1.0
N B:GLY70 4.9 5.8 1.0
N B:HIS69 4.9 5.0 1.0
C B:HIS69 4.9 5.9 1.0
CA B:HIS61 4.9 4.9 1.0
N B:ASP81 5.0 3.4 1.0

Reference:

V.Calderone, A.Casini, S.Mangani, L.Messori, P.L.Orioli. Structural Investigation of Cisplatin-Protein Interactions: Selective Platination of HIS19 in A Cuprozinc Superoxide Dismutase. Angew. Chem. Int. Ed. Engl. V. 45 1267 2006.
ISSN: ISSN 1433-7851
PubMed: 16416478
DOI: 10.1002/ANIE.200502599
Page generated: Wed Dec 16 03:17:12 2020

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