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Copper in PDB 3hw7: High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms

Enzymatic activity of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms

All present enzymatic activity of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms:
1.15.1.1;

Protein crystallography data

The structure of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms, PDB code: 3hw7 was solved by I.Ascone, C.Savino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.89 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.845, 50.509, 146.377, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 21.8

Other elements in 3hw7:

The structure of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms (pdb code 3hw7). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms, PDB code: 3hw7:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3hw7

Go back to Copper Binding Sites List in 3hw7
Copper binding site 1 out of 3 in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu152

b:17.5
occ:1.00
 ND1 A:HIS44 2.0 11.8 1.0
NE2 A:HIS118 2.0 20.2 1.0
NE2 A:HIS46 2.0 12.7 1.0
CD2 A:HIS118 2.9 17.9 1.0
CE1 A:HIS44 3.0 12.0 1.0
CD2 A:HIS46 3.0 10.4 1.0
CG A:HIS44 3.0 13.8 1.0
CE1 A:HIS46 3.1 15.0 1.0
CE1 A:HIS118 3.1 18.3 1.0
CB A:HIS44 3.4 13.3 1.0
NE2 A:HIS61 3.4 16.1 1.0
CD2 A:HIS61 3.6 16.1 1.0
CB A:VAL116 3.8 15.9 1.0
O A:HOH221 3.9 21.8 1.0
CG1 A:VAL116 4.0 14.1 1.0
N A:HIS44 4.1 14.4 1.0
NE2 A:HIS44 4.1 14.4 1.0
CG A:HIS118 4.1 19.8 1.0
CD2 A:HIS44 4.1 11.9 1.0
ND1 A:HIS118 4.1 19.4 1.0
ND1 A:HIS46 4.1 12.8 1.0
CG A:HIS46 4.2 13.3 1.0
CA A:HIS44 4.2 13.9 1.0
O A:HOH214 4.2 20.9 1.0
O A:VAL116 4.2 16.7 1.0
O A:HIS44 4.3 13.7 1.0
CE1 A:HIS61 4.3 17.1 1.0
C A:HIS44 4.5 14.0 1.0
CG A:HIS61 4.6 16.7 1.0
CG2 A:VAL116 4.7 14.2 1.0
C A:VAL116 4.7 16.1 1.0
CA A:VAL116 4.9 15.4 1.0
C A:PHE43 4.9 15.3 1.0
ND1 A:HIS61 4.9 17.3 1.0

Copper binding site 2 out of 3 in 3hw7

Go back to Copper Binding Sites List in 3hw7
Copper binding site 2 out of 3 in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu152

b:14.1
occ:0.60
 CU B:CU153 1.4 5.6 0.4
NE2 B:HIS46 1.9 10.8 1.0
NE2 B:HIS118 1.9 11.3 1.0
ND1 B:HIS44 2.1 11.7 1.0
CD2 B:HIS46 2.8 9.7 1.0
CD2 B:HIS118 2.8 12.1 1.0
CG B:HIS44 2.9 13.7 1.0
CE1 B:HIS118 3.0 9.7 1.0
CE1 B:HIS46 3.0 10.4 1.0
CB B:HIS44 3.1 11.5 1.0
NE2 B:HIS61 3.2 15.6 1.0
CE1 B:HIS44 3.2 11.1 1.0
CD2 B:HIS61 3.6 13.9 1.0
O B:HOH398 3.6 20.2 1.0
CB B:VAL116 3.7 12.2 1.0
CG1 B:VAL116 3.8 11.9 1.0
CG B:HIS46 4.0 12.2 1.0
CG B:HIS118 4.0 11.4 1.0
ND1 B:HIS46 4.0 8.9 1.0
ND1 B:HIS118 4.0 9.9 1.0
N B:HIS44 4.0 11.3 1.0
CA B:HIS44 4.0 11.4 1.0
O B:VAL116 4.2 12.7 1.0
CD2 B:HIS44 4.2 12.1 1.0
CE1 B:HIS61 4.3 15.8 1.0
NE2 B:HIS44 4.3 15.3 1.0
O B:HIS44 4.3 11.1 1.0
C B:HIS44 4.5 10.6 1.0
C B:VAL116 4.6 12.9 1.0
CG2 B:VAL116 4.6 14.1 1.0
CA B:VAL116 4.8 13.0 1.0
CG B:HIS61 4.8 11.5 1.0
C B:PHE43 4.9 11.6 1.0

Copper binding site 3 out of 3 in 3hw7

Go back to Copper Binding Sites List in 3hw7
Copper binding site 3 out of 3 in the High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of High Pressure (0.57 Gpa) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase at 2.0 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu153

b:5.6
occ:0.40
 CU B:CU1152 1.4 14.1 0.6
NE2 B:HIS61 2.0 15.6 1.0
ND1 B:HIS44 2.0 11.7 1.0
NE2 B:HIS46 2.2 10.8 1.0
NE2 B:HIS118 2.3 11.3 1.0
O B:HOH398 2.6 20.2 1.0
CD2 B:HIS61 2.7 13.9 1.0
CE1 B:HIS44 2.9 11.1 1.0
CE1 B:HIS46 2.9 10.4 1.0
CG B:HIS44 3.0 13.7 1.0
CE1 B:HIS118 3.0 9.7 1.0
CE1 B:HIS61 3.1 15.8 1.0
CD2 B:HIS118 3.3 12.1 1.0
CD2 B:HIS46 3.4 9.7 1.0
CB B:HIS44 3.4 11.5 1.0
CG B:HIS61 3.9 11.5 1.0
NE2 B:HIS44 3.9 15.3 1.0
CD2 B:HIS44 4.0 12.1 1.0
ND1 B:HIS61 4.1 13.4 1.0
ND1 B:HIS46 4.1 8.9 1.0
ND1 B:HIS118 4.1 9.9 1.0
CG B:HIS46 4.3 12.2 1.0
CG B:HIS118 4.3 11.4 1.0
O B:HOH225 4.7 13.8 1.0
CA B:HIS44 4.7 11.4 1.0
CG1 B:VAL116 4.9 11.9 1.0
N B:HIS44 4.9 11.3 1.0
CB B:VAL116 5.0 12.2 1.0

Reference:

I.Ascone, C.Savino, R.Kahn, R.Fourme. Flexibility of the Cu,Zn Superoxide Dismutase Structure Investigated at 0.57 Gpa Acta Crystallogr.,Sect.D V. 66 654 2010.
ISSN: ISSN 0907-4449
PubMed: 20516618
DOI: 10.1107/S0907444910012321
Page generated: Sun Dec 13 11:10:01 2020

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