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Zinc in PDB 1eso: Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli

Enzymatic activity of Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli

All present enzymatic activity of Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli:
1.15.1.1;

Protein crystallography data

The structure of Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli, PDB code: 1eso was solved by A.Pesce, C.Capasso, A.Battistoni, S.Folcarelli, G.Rotilio, A.Desideri, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 33.000, 52.400, 43.200, 90.00, 111.20, 90.00
R / Rfree (%) 16.8 / 26.3

Other elements in 1eso:

The structure of Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli also contains other interesting chemical elements:

Copper (Cu) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli (pdb code 1eso). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli, PDB code: 1eso:

Zinc binding site 1 out of 1 in 1eso

Go back to Zinc Binding Sites List in 1eso
Zinc binding site 1 out of 1 in the Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn149

b:22.9
occ:1.00
ND1 A:HIS78 1.9 25.6 1.0
ND1 A:HIS69 2.0 15.4 1.0
OD1 A:ASP81 2.1 22.4 1.0
ND1 A:HIS61 2.1 18.5 1.0
CE1 A:HIS69 2.7 14.1 1.0
CE1 A:HIS78 2.9 20.6 1.0
CG A:ASP81 3.0 28.8 1.0
CG A:HIS78 3.0 19.9 1.0
CE1 A:HIS61 3.0 25.4 1.0
CG A:HIS69 3.2 22.6 1.0
CG A:HIS61 3.2 23.7 1.0
OD2 A:ASP81 3.2 21.0 1.0
CB A:HIS78 3.4 15.9 1.0
CB A:HIS61 3.6 16.7 1.0
CB A:HIS69 3.7 20.6 1.0
NE2 A:HIS69 3.9 15.7 1.0
CA A:HIS69 4.0 19.3 1.0
NE2 A:HIS78 4.0 23.6 1.0
CD2 A:HIS78 4.1 24.1 1.0
CD2 A:HIS69 4.2 19.3 1.0
NE2 A:HIS61 4.2 22.9 1.0
CD2 A:HIS61 4.3 22.1 1.0
CB A:ASP81 4.3 16.3 1.0
CA A:ASP81 4.7 18.4 1.0
CA A:HIS78 4.8 17.4 1.0
O A:LYS68 4.8 21.3 1.0
N A:ASP81 4.9 15.7 1.0
C A:HIS69 4.9 19.4 1.0
CD2 A:HIS44 4.9 14.8 1.0
N A:HIS69 5.0 19.5 1.0

Reference:

A.Pesce, C.Capasso, A.Battistoni, S.Folcarelli, G.Rotilio, A.Desideri, M.Bolognesi. Unique Structural Features of the Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli, Revealed By X-Ray Crystallography. J.Mol.Biol. V. 274 408 1997.
ISSN: ISSN 0022-2836
PubMed: 9405149
DOI: 10.1006/JMBI.1997.1400
Page generated: Wed Dec 16 02:48:31 2020

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