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Copper 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
Chlorine (Cl) 4 atoms
Zinc (Zn) 2 atoms

Copper Binding Sites:

The binding sites of Copper 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 Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Cisplatinated Bovine Cu,Zn Superoxide Dismutase, PDB code: 2aeo:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2aeo

Go back to Copper Binding Sites List in 2aeo
Copper 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 Copper with other atoms in the Cu 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:Cu152

b:12.8
occ:1.00
NE2 A:HIS118 2.1 2.3 1.0
ND1 A:HIS44 2.1 3.7 1.0
NE2 A:HIS61 2.1 6.2 1.0
NE2 A:HIS46 2.2 2.0 1.0
O A:HOH294 2.8 7.8 1.0
CG A:HIS44 2.9 5.0 1.0
CD2 A:HIS61 3.0 4.1 1.0
CD2 A:HIS118 3.0 3.7 1.0
CE1 A:HIS118 3.1 2.0 1.0
CE1 A:HIS46 3.1 2.5 1.0
CB A:HIS44 3.1 3.1 1.0
CD2 A:HIS46 3.2 2.0 1.0
CE1 A:HIS44 3.2 5.2 1.0
CE1 A:HIS61 3.2 5.2 1.0
ND1 A:HIS118 4.1 5.6 1.0
CG A:HIS118 4.1 4.5 1.0
CD2 A:HIS44 4.1 4.8 1.0
CG A:HIS61 4.2 4.6 1.0
ND1 A:HIS46 4.2 3.4 1.0
NE2 A:HIS44 4.2 2.4 1.0
ND1 A:HIS61 4.2 3.6 1.0
CG A:HIS46 4.3 2.0 1.0
CA A:HIS44 4.5 3.6 1.0
O A:HOH291 4.6 6.8 1.0
CB A:VAL116 4.8 2.3 1.0
CG1 A:VAL116 4.8 3.3 1.0
N A:HIS44 4.9 3.6 1.0
O A:HOH295 4.9 2.0 1.0

Copper binding site 2 out of 2 in 2aeo

Go back to Copper Binding Sites List in 2aeo
Copper 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 Copper with other atoms in the Cu 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:Cu152

b:15.3
occ:1.00
ND1 B:HIS44 2.1 3.6 1.0
NE2 B:HIS118 2.2 5.0 1.0
NE2 B:HIS46 2.2 2.0 1.0
NE2 B:HIS61 2.3 6.9 1.0
O B:HOH294 2.8 4.8 1.0
CG B:HIS44 3.0 4.5 1.0
CD2 B:HIS61 3.0 6.2 1.0
CD2 B:HIS118 3.0 2.7 1.0
CE1 B:HIS46 3.1 3.5 1.0
CE1 B:HIS118 3.2 3.8 1.0
CB B:HIS44 3.2 2.6 1.0
CE1 B:HIS44 3.2 3.7 1.0
CD2 B:HIS46 3.2 2.0 1.0
CE1 B:HIS61 3.5 8.0 1.0
CG B:HIS118 4.2 3.5 1.0
CD2 B:HIS44 4.2 7.4 1.0
ND1 B:HIS118 4.2 3.4 1.0
CG B:HIS61 4.2 5.9 1.0
ND1 B:HIS46 4.2 2.8 1.0
NE2 B:HIS44 4.2 4.3 1.0
CG B:HIS46 4.3 4.0 1.0
ND1 B:HIS61 4.4 7.9 1.0
CA B:HIS44 4.5 2.8 1.0
O B:HOH311 4.6 7.6 1.0
CG1 B:VAL116 4.7 2.0 1.0
N B:HIS44 4.8 2.5 1.0
CB B:VAL116 4.8 2.7 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: Sun Dec 13 11:03:26 2020

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