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Copper in PDB 1sxs: Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate

Enzymatic activity of Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate

All present enzymatic activity of Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate:
1.15.1.1;

Protein crystallography data

The structure of Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate, PDB code: 1sxs was solved by M.Ferraroni, W.R.Rypniewski, B.Bruni, P.Orioli, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 104.600, 197.500, 50.800, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / n/a

Other elements in 1sxs:

The structure of Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Zinc (Zn) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate (pdb code 1sxs). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate, PDB code: 1sxs:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1sxs

Go back to Copper Binding Sites List in 1sxs
Copper binding site 1 out of 2 in the Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu152

b:24.2
occ:0.99
NE2 A:HIS118 2.1 13.3 1.0
ND1 A:HIS44 2.1 11.2 1.0
NE2 A:HIS61 2.2 16.6 1.0
NE2 A:HIS46 2.3 18.2 1.0
N A:SCN155 2.6 37.6 1.0
CE1 A:HIS118 2.9 4.2 1.0
CG A:HIS44 2.9 11.0 1.0
CE1 A:HIS46 3.0 7.7 1.0
CD2 A:HIS61 3.1 10.9 1.0
CD2 A:HIS118 3.1 11.9 1.0
CE1 A:HIS44 3.1 14.1 1.0
CB A:HIS44 3.2 5.8 1.0
CE1 A:HIS61 3.3 8.0 1.0
C A:SCN155 3.4 45.5 1.0
CD2 A:HIS46 3.4 11.1 1.0
ND1 A:HIS118 4.1 5.1 1.0
CD2 A:HIS44 4.1 12.3 1.0
NE2 A:HIS44 4.2 9.3 1.0
CG A:HIS118 4.2 4.7 1.0
ND1 A:HIS46 4.2 14.5 1.0
CG A:HIS61 4.2 8.1 1.0
ND1 A:HIS61 4.3 9.9 1.0
CG A:HIS46 4.4 11.6 1.0
CA A:HIS44 4.5 5.8 1.0
N A:HIS44 4.6 4.8 1.0
CG1 A:VAL116 4.7 7.8 1.0
S A:SCN155 4.7 44.9 1.0
CB A:VAL116 4.7 11.2 1.0
O A:HOH163 4.8 13.3 1.0

Copper binding site 2 out of 2 in 1sxs

Go back to Copper Binding Sites List in 1sxs
Copper binding site 2 out of 2 in the Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Thiocyanate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu152

b:39.5
occ:0.99
ND1 B:HIS44 1.9 32.5 1.0
NE2 B:HIS118 2.1 25.8 1.0
NE2 B:HIS61 2.3 39.0 1.0
NE2 B:HIS46 2.4 24.2 1.0
N B:SCN155 2.5 64.8 1.0
CG B:HIS44 2.8 35.3 1.0
CE1 B:HIS118 3.0 25.6 1.0
CE1 B:HIS44 3.0 34.5 1.0
CD2 B:HIS61 3.0 39.4 1.0
C B:SCN155 3.1 70.4 1.0
CD2 B:HIS118 3.1 20.7 1.0
CB B:HIS44 3.1 24.7 1.0
CE1 B:HIS46 3.2 26.1 1.0
CE1 B:HIS61 3.4 36.9 1.0
CD2 B:HIS46 3.4 18.2 1.0
CD2 B:HIS44 4.0 28.0 1.0
NE2 B:HIS44 4.0 36.9 1.0
ND1 B:HIS118 4.1 24.2 1.0
CG B:HIS118 4.2 21.6 1.0
CG B:HIS61 4.2 31.7 1.0
ND1 B:HIS61 4.3 30.4 1.0
ND1 B:HIS46 4.3 22.3 1.0
CA B:HIS44 4.4 23.3 1.0
CG B:HIS46 4.4 21.5 1.0
S B:SCN155 4.5 80.1 1.0
N B:HIS44 4.5 24.6 1.0
CB B:VAL116 4.6 22.1 1.0
CG1 B:VAL116 4.7 19.4 1.0
O B:HIS44 4.9 24.3 1.0
O B:HOH195 4.9 53.3 1.0
C B:HIS44 4.9 24.8 1.0

Reference:

M.Ferraroni, W.R.Rypniewski, B.Bruni, P.Orioli, S.Mangani. Crystallographic Determination of Reduced Bovine Superoxide Dismutase at pH 5.0 and of Anion Binding to Its Active Site J.Biol.Inorg.Chem. V. 3 411 1998.
ISSN: ISSN 0949-8257
Page generated: Mon Jul 14 00:27:42 2025

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