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Zinc in PDB 4l05: Cu/Zn Superoxide Dismutase From Brucella Abortus

Enzymatic activity of Cu/Zn Superoxide Dismutase From Brucella Abortus

All present enzymatic activity of Cu/Zn Superoxide Dismutase From Brucella Abortus:
1.15.1.1;

Protein crystallography data

The structure of Cu/Zn Superoxide Dismutase From Brucella Abortus, PDB code: 4l05 was solved by D.S.Shin, M.Didonato, A.J.Pratt, C.K.Bruns, D.E.Cabelli, J.S.Kroll, C.A.Belzer, L.B.Tabatabai, J.A.Tainer, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.04 / 1.10
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 49.910, 70.528, 80.359, 90.00, 90.00, 90.00
R / Rfree (%) 11.3 / 11.8

Other elements in 4l05:

The structure of Cu/Zn Superoxide Dismutase From Brucella Abortus also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cu/Zn Superoxide Dismutase From Brucella Abortus (pdb code 4l05). 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 Cu/Zn Superoxide Dismutase From Brucella Abortus, PDB code: 4l05:

Zinc binding site 1 out of 1 in 4l05

Go back to Zinc Binding Sites List in 4l05
Zinc binding site 1 out of 1 in the Cu/Zn Superoxide Dismutase From Brucella Abortus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cu/Zn Superoxide Dismutase From Brucella Abortus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn203

b:4.6
occ:0.95
OD1 A:ASP93 2.0 5.0 1.0
ND1 A:HIS73 2.0 7.3 0.6
ND1 A:HIS90 2.0 5.2 1.0
ND1 A:HIS73 2.1 7.3 0.4
ND1 A:HIS82 2.1 4.8 1.0
CG A:ASP93 2.8 5.1 1.0
HB2 A:HIS90 2.9 6.5 1.0
CE1 A:HIS73 2.9 10.8 0.6
CE1 A:HIS82 2.9 4.8 1.0
OD2 A:ASP93 2.9 5.4 1.0
CE1 A:HIS73 3.0 10.6 0.4
CE1 A:HIS90 3.0 5.4 1.0
HE1 A:HIS82 3.0 5.8 1.0
HE1 A:HIS73 3.0 12.9 0.6
CG A:HIS73 3.1 8.3 0.6
CG A:HIS90 3.1 5.0 1.0
HE1 A:HIS73 3.1 12.7 0.4
CG A:HIS73 3.1 8.4 0.4
HE1 A:HIS90 3.1 6.4 1.0
CG A:HIS82 3.1 4.4 1.0
HA A:HIS82 3.2 5.7 1.0
HB2 A:HIS82 3.3 5.4 1.0
HB3 A:HIS73 3.3 8.6 0.6
HB3 A:HIS73 3.4 8.6 0.4
HB2 A:HIS73 3.4 8.6 0.6
CB A:HIS90 3.4 5.4 1.0
HB2 A:HIS73 3.4 8.6 0.4
CB A:HIS73 3.5 7.2 0.6
CB A:HIS73 3.5 7.1 0.4
CB A:HIS82 3.6 4.5 1.0
HB3 A:HIS90 3.7 6.5 1.0
CA A:HIS82 3.9 4.7 1.0
NE2 A:HIS73 4.0 13.4 0.6
HD23 A:LEU141 4.0 13.2 1.0
NE2 A:HIS82 4.1 4.7 1.0
NE2 A:HIS73 4.1 13.1 0.4
NE2 A:HIS90 4.1 5.9 1.0
CD2 A:HIS73 4.1 12.3 0.6
HD22 A:LEU141 4.1 13.2 1.0
CD2 A:HIS90 4.2 5.4 1.0
CB A:ASP93 4.2 5.0 1.0
CD2 A:HIS73 4.2 12.2 0.4
CD2 A:HIS82 4.2 4.7 1.0
HA A:ASP93 4.3 5.7 1.0
HB3 A:HIS82 4.5 5.4 1.0
CD2 A:LEU141 4.5 11.0 1.0
H A:HIS90 4.6 6.6 1.0
H A:LEU83 4.6 5.8 1.0
HB3 A:ASP93 4.6 6.0 1.0
CA A:ASP93 4.7 4.7 1.0
HB3 A:HIS48 4.7 6.7 1.0
HA A:LEU141 4.7 7.0 1.0
HB2 A:ASP93 4.8 6.0 1.0
H A:GLY84 4.8 5.7 1.0
CA A:HIS90 4.8 5.1 1.0
HD2 A:HIS48 4.8 6.5 1.0
HE2 A:HIS73 4.8 16.1 0.6
HE2 A:HIS82 4.8 5.7 1.0
N A:HIS82 4.8 4.8 1.0
CD2 A:HIS48 4.9 5.4 1.0
C A:HIS82 4.9 4.9 1.0
HE2 A:HIS90 4.9 7.0 1.0
H A:ASP93 4.9 5.8 1.0
N A:ASP93 4.9 4.8 1.0
HD21 A:LEU141 5.0 13.2 1.0
O A:HIS81 5.0 5.8 1.0

Reference:

D.S.Shin, M.Didonato, A.J.Pratt, C.J.Kassmann, C.K.Bruns, D.E.Cabelli, J.S.Kroll, C.A.Belzer, L.B.Tabatabai, J.A.Tainer, E.D.Getzoff. Structural and Biochemical Characterization of Dimeric and Monomeric Cu,Zn Superoxide Dismutases From the Pathogens Neisseria Meningitidis and Brucella Abortus To Be Published.
Page generated: Sun Oct 27 01:27:50 2024

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