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Copper in PDB 1e9p: Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3)

Enzymatic activity of Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3)

All present enzymatic activity of Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3):
1.13.1.1;

Protein crystallography data

The structure of Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3), PDB code: 1e9p was solved by M.A.Hough, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75 / 1.7
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.800, 51.100, 148.000, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 20.2

Other elements in 1e9p:

The structure of Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3) also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3) (pdb code 1e9p). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3), PDB code: 1e9p:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 1e9p

Go back to Copper Binding Sites List in 1e9p
Copper binding site 1 out of 3 in the Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3)


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 Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu152

b:32.5
occ:1.00
NE2 A:HIS118 2.0 15.8 1.0
NE2 A:HIS46 2.1 16.3 1.0
ND1 A:HIS44 2.3 18.1 1.0
O A:HOH2019 2.4 54.3 0.5
NE2 A:HIS61 2.8 22.1 1.0
CD2 A:HIS118 2.9 19.3 1.0
CE1 A:HIS46 2.9 16.9 1.0
CE1 A:HIS118 3.0 20.2 1.0
CG A:HIS44 3.2 17.2 1.0
CD2 A:HIS46 3.2 15.9 1.0
CD2 A:HIS61 3.2 19.8 1.0
O A:HOH2071 3.3 17.8 0.5
CE1 A:HIS44 3.3 19.3 1.0
CB A:HIS44 3.4 17.2 1.0
CE1 A:HIS61 3.9 21.4 1.0
ND1 A:HIS118 4.0 19.4 1.0
CG A:HIS118 4.0 18.0 1.0
ND1 A:HIS46 4.1 14.6 1.0
CG A:HIS46 4.2 14.4 1.0
CD2 A:HIS44 4.3 18.3 1.0
NE2 A:HIS44 4.4 18.6 1.0
CB A:VAL116 4.4 15.5 1.0
CG A:HIS61 4.4 18.6 1.0
CG1 A:VAL116 4.5 16.6 1.0
CA A:HIS44 4.6 14.9 1.0
N A:HIS44 4.7 13.4 1.0
ND1 A:HIS61 4.8 19.2 1.0
CG2 A:VAL116 5.0 15.5 1.0
O A:HIS44 5.0 15.4 1.0

Copper binding site 2 out of 3 in 1e9p

Go back to Copper Binding Sites List in 1e9p
Copper binding site 2 out of 3 in the Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3)


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 Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu153

b:17.0
occ:1.00
ND1 A:HIS61 2.0 19.2 1.0
ND1 A:HIS78 2.0 15.5 1.0
ND1 A:HIS69 2.0 17.2 1.0
OD1 A:ASP81 2.0 16.3 1.0
CG A:ASP81 2.7 16.8 1.0
CE1 A:HIS78 2.8 15.7 1.0
OD2 A:ASP81 2.8 17.3 1.0
CE1 A:HIS61 2.9 21.4 1.0
CE1 A:HIS69 2.9 17.3 1.0
CG A:HIS61 3.0 18.6 1.0
CG A:HIS78 3.1 13.8 1.0
CG A:HIS69 3.1 18.8 1.0
CB A:HIS61 3.4 16.9 1.0
CB A:HIS78 3.6 14.2 1.0
CB A:HIS69 3.6 18.7 1.0
O A:LYS134 4.0 24.6 1.0
NE2 A:HIS78 4.0 16.1 1.0
CA A:HIS69 4.0 18.8 1.0
NE2 A:HIS61 4.0 22.1 1.0
NE2 A:HIS69 4.1 17.5 1.0
CD2 A:HIS61 4.1 19.8 1.0
CD2 A:HIS78 4.1 15.6 1.0
CB A:ASP81 4.2 15.5 1.0
CD2 A:HIS69 4.2 18.1 1.0
O A:HOH2070 4.5 23.9 1.0
CA A:ASP81 4.7 15.7 1.0
N A:HIS78 4.7 16.3 1.0
CA A:HIS78 4.8 14.9 1.0
N A:GLY70 4.8 19.4 1.0
N A:ASP81 4.9 15.7 1.0
C A:HIS69 4.9 20.4 1.0
C A:LYS134 4.9 25.1 1.0
CA A:HIS61 5.0 15.3 1.0
N A:HIS69 5.0 19.6 1.0
CD2 A:HIS44 5.0 18.3 1.0

Copper binding site 3 out of 3 in 1e9p

Go back to Copper Binding Sites List in 1e9p
Copper binding site 3 out of 3 in the Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Bovine Cu, Zn Sod to 1.7 Angstrom (3 of 3) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu152

b:20.2
occ:1.00
CD2 B:HIS44 2.0 11.0 1.0
NE2 B:HIS61 2.1 15.2 1.0
NE2 B:HIS118 2.1 13.2 1.0
NE2 B:HIS46 2.2 14.8 1.0
O B:HOH2029 2.4 22.5 1.0
CG B:HIS44 2.9 13.9 1.0
CE1 B:HIS46 2.9 15.3 1.0
CD2 B:HIS61 2.9 15.9 1.0
CE1 B:HIS118 3.0 13.6 1.0
NE2 B:HIS44 3.1 18.4 1.0
CD2 B:HIS118 3.1 14.3 1.0
CE1 B:HIS61 3.2 15.8 1.0
CD2 B:HIS46 3.3 14.1 1.0
CB B:HIS44 3.3 13.6 1.0
ND1 B:HIS44 4.1 16.0 1.0
ND1 B:HIS46 4.1 13.6 1.0
CE1 B:HIS44 4.1 13.0 1.0
ND1 B:HIS118 4.1 11.9 1.0
CG B:HIS61 4.1 13.3 1.0
CG B:HIS118 4.2 12.0 1.0
ND1 B:HIS61 4.2 13.6 1.0
CG B:HIS46 4.3 13.1 1.0
O B:HOH2088 4.5 23.6 1.0
CA B:HIS44 4.7 12.0 1.0
O B:HOH2085 4.8 19.4 1.0
N B:HIS44 4.9 12.1 1.0
CB B:VAL116 4.9 13.8 1.0
CG1 B:VAL116 4.9 16.6 1.0

Reference:

M.A.Hough, R.W.Strange, S.S.Hasnain. Conformational Variability of the Cu Site in One Subunit of Bovine Cuzn Superoxide Dismutase: the Importance of Mobility in the GLU119-LEU142 Loop Region For Catalytic Function. J.Mol.Biol. V. 304 231 2000.
ISSN: ISSN 0022-2836
PubMed: 11080458
DOI: 10.1006/JMBI.2000.4186
Page generated: Sun Dec 13 10:58:31 2020

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