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Zinc in PDB 1sxz: Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Azide

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

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

Protein crystallography data

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

Resolution Low / High (Å) 10.00 / 2.05
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 (%) 16.6 / n/a

Other elements in 1sxz:

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

Copper (Cu) 2 atoms
Calcium (Ca) 2 atoms

Zinc Binding Sites:

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

Zinc binding site 1 out of 2 in 1sxz

Go back to Zinc Binding Sites List in 1sxz
Zinc binding site 1 out of 2 in the Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Azide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Azide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn153

b:10.4
occ:1.00
ND1 A:HIS78 1.9 2.1 1.0
OD1 A:ASP81 1.9 11.8 1.0
ND1 A:HIS61 2.0 12.8 1.0
ND1 A:HIS69 2.1 5.0 1.0
CE1 A:HIS78 2.8 9.3 1.0
CG A:ASP81 2.8 10.8 1.0
OD2 A:ASP81 2.9 13.9 1.0
CE1 A:HIS69 3.0 10.2 1.0
CE1 A:HIS61 3.0 11.3 1.0
CG A:HIS61 3.0 11.6 1.0
CG A:HIS78 3.1 7.0 1.0
CG A:HIS69 3.2 2.1 1.0
CB A:HIS61 3.4 7.2 1.0
CB A:HIS78 3.6 4.6 1.0
CB A:HIS69 3.6 5.7 1.0
O A:LYS134 3.9 12.9 1.0
NE2 A:HIS78 3.9 5.7 1.0
CA A:HIS69 4.0 7.3 1.0
CD2 A:HIS78 4.1 5.5 1.0
NE2 A:HIS61 4.1 19.1 1.0
NE2 A:HIS69 4.1 7.9 1.0
CD2 A:HIS61 4.2 11.3 1.0
CB A:ASP81 4.2 7.1 1.0
CD2 A:HIS69 4.3 4.9 1.0
CA A:ASP81 4.7 8.0 1.0
N A:HIS78 4.7 6.7 1.0
O A:HOH160 4.8 12.9 1.0
C A:LYS134 4.8 9.5 1.0
CA A:HIS78 4.8 5.1 1.0
N A:GLY70 4.9 6.5 1.0
CA A:HIS61 4.9 9.4 1.0
N A:ASP81 4.9 8.8 1.0
N A:HIS69 4.9 11.2 1.0
C A:HIS69 5.0 8.5 1.0

Zinc binding site 2 out of 2 in 1sxz

Go back to Zinc Binding Sites List in 1sxz
Zinc binding site 2 out of 2 in the Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Azide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Reduced Bovine Superoxide Dismutase at pH 5.0 Complexed with Azide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn153

b:27.4
occ:1.00
OD1 B:ASP81 1.8 17.2 1.0
ND1 B:HIS78 1.9 18.3 1.0
ND1 B:HIS61 2.2 35.4 1.0
ND1 B:HIS69 2.3 32.3 1.0
CG B:ASP81 2.7 29.5 1.0
CE1 B:HIS78 2.9 21.9 1.0
OD2 B:ASP81 2.9 29.1 1.0
CG B:HIS78 3.0 22.4 1.0
CG B:HIS61 3.1 31.3 1.0
CE1 B:HIS69 3.2 39.7 1.0
CE1 B:HIS61 3.2 39.6 1.0
CG B:HIS69 3.3 29.2 1.0
CB B:HIS61 3.4 24.9 1.0
CB B:HIS78 3.4 21.4 1.0
CB B:HIS69 3.6 24.7 1.0
O B:LYS134 3.8 36.2 1.0
CA B:HIS69 3.9 26.2 1.0
NE2 B:HIS78 4.0 22.8 1.0
CD2 B:HIS78 4.1 21.9 1.0
CB B:ASP81 4.1 21.5 1.0
CD2 B:HIS61 4.3 40.3 1.0
NE2 B:HIS61 4.3 41.1 1.0
NE2 B:HIS69 4.3 43.0 1.0
CD2 B:HIS69 4.4 33.7 1.0
O B:HOH162 4.6 32.5 1.0
CA B:ASP81 4.6 24.7 1.0
N B:HIS78 4.7 30.2 1.0
N B:ASP81 4.7 25.7 1.0
CA B:HIS78 4.8 26.9 1.0
N B:GLY70 4.8 30.4 1.0
N B:HIS69 4.9 30.4 1.0
C B:HIS69 4.9 32.7 1.0
CA B:HIS61 4.9 21.0 1.0
C B:LYS134 4.9 35.0 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: Wed Dec 16 03:03:59 2020

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