Copper in PDB 1eso: 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;

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

The binding sites of Copper 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 Copper atom.
In total only one binding site of Copper was determined in the Monomeric Cu,Zn Superoxide Dismutase From Escherichia Coli, PDB code: 1eso:

Copper 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 Copper with other atoms in the Cu 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:Cu150 b:30.8 occ:1.00 NE2 A:HIS46 2.1 20.7 1.0 NE2 A:HIS118 2.1 22.2 1.0 ND1 A:HIS44 2.2 17.5 1.0 NE2 A:HIS61 2.7 22.9 1.0 CD2 A:HIS118 3.0 15.6 1.0 CE1 A:HIS46 3.0 16.9 1.0 CG A:HIS44 3.1 12.7 1.0 CD2 A:HIS46 3.1 20.2 1.0 CE1 A:HIS118 3.1 24.5 1.0 CD2 A:HIS61 3.2 22.1 1.0 CE1 A:HIS44 3.2 13.5 1.0 CB A:HIS44 3.3 11.3 1.0 CE1 A:HIS61 3.7 25.4 1.0 CG A:HIS118 4.1 20.3 1.0 ND1 A:HIS46 4.1 19.9 1.0 ND1 A:HIS118 4.2 26.0 1.0 CG A:HIS46 4.2 15.4 1.0 CD2 A:HIS44 4.3 14.8 1.0 CB A:MET116 4.3 19.3 1.0 NE2 A:HIS44 4.3 14.7 1.0 O A:HOH220 4.4 45.9 1.0 CA A:HIS44 4.4 17.9 1.0 CG A:HIS61 4.4 23.7 1.0 CG A:MET116 4.5 19.8 1.0 N A:HIS44 4.5 17.6 1.0 ND1 A:HIS61 4.6 18.5 1.0 O A:HOH199 4.6 39.3 1.0 O A:HIS44 4.7 29.5 1.0 C A:HIS44 4.7 21.4 1.0

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