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Zinc in PDB 1oal: Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase

Enzymatic activity of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase

All present enzymatic activity of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase, PDB code: 1oal was solved by P.Cioni, A.Pesce, B.M.D.Rocca, L.Castellifalconiparrilli, M.Bolognesi, G.Strambini, A.Desideri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.50
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 86.100, 86.100, 97.800, 90.00, 90.00, 120.00
R / Rfree (%) 15.6 / 19.4

Other elements in 1oal:

The structure of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase also contains other interesting chemical elements:

Copper (Cu) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase (pdb code 1oal). 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 Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase, PDB code: 1oal:

Zinc binding site 1 out of 1 in 1oal

Go back to Zinc Binding Sites List in 1oal
Zinc binding site 1 out of 1 in the Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Active Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn152

b:15.8
occ:1.00
 OD1 A:ASP91 2.0 14.9 1.0
ND1 A:HIS88 2.0 14.9 1.0
ND1 A:HIS70 2.0 17.6 1.0
ND1 A:HIS79 2.1 15.4 1.0
CG A:ASP91 2.8 14.3 1.0
CE1 A:HIS88 2.9 18.0 1.0
CE1 A:HIS79 2.9 15.6 1.0
OD2 A:ASP91 2.9 14.9 1.0
CE1 A:HIS70 3.0 21.5 1.0
CG A:HIS88 3.1 15.8 1.0
CG A:HIS70 3.1 16.3 1.0
CG A:HIS79 3.2 14.7 1.0
CB A:HIS88 3.4 16.6 1.0
CB A:HIS70 3.5 16.4 1.0
CB A:HIS79 3.6 16.8 1.0
CA A:HIS79 3.8 15.9 1.0
NE2 A:HIS88 4.1 17.4 1.0
NE2 A:HIS79 4.1 15.1 1.0
NE2 A:HIS70 4.1 19.3 1.0
CD2 A:HIS88 4.1 17.3 1.0
CD2 A:HIS70 4.2 20.4 1.0
CB A:ASP91 4.2 13.5 1.0
CD2 A:HIS79 4.2 15.9 1.0
CD2 A:LEU138 4.6 29.5 1.0
N A:GLY80 4.6 15.5 1.0
O A:LYS78 4.7 17.5 1.0
CA A:ASP91 4.7 13.9 1.0
CA A:HIS88 4.7 16.0 1.0
C A:HIS79 4.8 17.4 1.0
N A:HIS79 4.8 16.8 1.0
CD2 A:HIS45 4.8 15.7 1.0
N A:HIS88 4.8 15.7 1.0
N A:ASP91 4.9 14.5 1.0
CA A:HIS70 5.0 16.1 1.0

Reference:

P.Cioni, A.Pesce, B.Morozzo Della Rocca, S.Castelli, M.Falconi, L.Parrilli, M.Bolognesi, G.Strambini, A.Desideri. Active-Site Copper and Zinc Ions Modulate the Quaternary Structure of Prokaryotic Cu,Zn Superoxide Dismutase J.Mol.Biol. V. 326 1351 2003.
ISSN: ISSN 0022-2836
PubMed: 12595249
DOI: 10.1016/S0022-2836(03)00047-0
Page generated: Wed Oct 16 17:28:36 2024

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