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

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

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

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

Zinc

(Zn)

1 atom

The binding sites of Copper atom in the Cu/Zn Superoxide Dismutase From Brucella Abortus (pdb code 4l05). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Cu/Zn Superoxide Dismutase From Brucella Abortus, PDB code: 4l05:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Cu/Zn Superoxide Dismutase From Brucella Abortus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu/Zn Superoxide Dismutase From Brucella Abortus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:9.3 occ:0.58 CU A:CU202 0.8 5.9 0.4 NE2 A:HIS50 2.0 6.3 1.0 ND1 A:HIS48 2.0 6.6 1.0 NE2 A:HIS128 2.1 6.8 1.0 NE2 A:HIS73 2.6 13.1 0.4 HE2 A:HIS73 2.6 16.1 0.6 HB2 A:HIS48 2.7 6.7 1.0 O A:HOH562 2.7 7.7 0.6 CE1 A:HIS50 2.9 5.2 1.0 CD2 A:HIS128 3.0 5.7 1.0 CE1 A:HIS48 3.0 5.6 1.0 CD2 A:HIS50 3.0 5.2 1.0 CG A:HIS48 3.0 5.4 1.0 HB3 A:MET126 3.1 5.7 1.0 NE2 A:HIS73 3.1 13.4 0.6 HD2 A:HIS128 3.1 6.8 1.0 CE1 A:HIS128 3.1 6.1 1.0 HE1 A:HIS50 3.1 6.2 1.0 HE1 A:HIS48 3.2 6.7 1.0 HD2 A:HIS50 3.2 6.2 1.0 HD2 A:HIS73 3.2 14.7 0.4 CD2 A:HIS73 3.3 12.2 0.4 CB A:HIS48 3.3 5.5 1.0 HE1 A:HIS128 3.4 7.3 1.0 HG2 A:MET126 3.4 6.2 1.0 CD2 A:HIS73 3.6 12.3 0.6 HD2 A:HIS73 3.6 14.8 0.6 CE1 A:HIS73 3.7 10.6 0.4 CB A:MET126 3.9 4.8 1.0 O A:HOH562 3.9 6.6 0.4 CE1 A:HIS73 3.9 10.8 0.6 HE1 A:HIS73 3.9 12.7 0.4 HB3 A:HIS48 4.0 6.7 1.0 CG A:MET126 4.0 5.1 1.0 ND1 A:HIS50 4.1 5.3 1.0 NE2 A:HIS48 4.1 5.4 1.0 CG A:HIS50 4.1 5.2 1.0 HB2 A:MET126 4.1 5.7 1.0 CD2 A:HIS48 4.1 5.4 1.0 CG A:HIS128 4.1 5.3 1.0 O A:HOH330 4.2 9.5 1.0 HE1 A:HIS73 4.2 12.9 0.6 ND1 A:HIS128 4.2 5.5 1.0 H A:HIS48 4.2 5.6 1.0 HG3 A:MET126 4.3 6.2 1.0 CA A:HIS48 4.4 5.0 1.0 N A:HIS48 4.4 4.6 1.0 CG A:HIS73 4.5 8.4 0.4 CG A:HIS73 4.6 8.3 0.6 ND1 A:HIS73 4.6 7.3 0.4 ND1 A:HIS73 4.7 7.3 0.6 O A:HIS48 4.7 5.3 1.0 O A:MET126 4.8 5.0 1.0 HD1 A:HIS50 4.8 6.3 1.0 O A:HOH395 4.8 18.9 1.0 C A:HIS48 4.8 5.0 1.0 HE2 A:HIS48 4.9 6.5 1.0 HG2 A:ARG147 4.9 6.7 1.0 HD1 A:HIS128 5.0 6.7 1.0 HD2 A:HIS48 5.0 6.5 1.0

Copper binding site 2 out of 2 in the Cu/Zn Superoxide Dismutase From Brucella Abortus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu/Zn Superoxide Dismutase From Brucella Abortus within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu202 b:5.9 occ:0.42 CU A:CU1201 0.8 9.3 0.6 HE2 A:HIS73 1.9 16.1 0.6 O A:HOH562 2.0 7.7 0.6 NE2 A:HIS73 2.1 13.1 0.4 ND1 A:HIS48 2.1 6.6 1.0 NE2 A:HIS50 2.2 6.3 1.0 NE2 A:HIS128 2.2 6.8 1.0 NE2 A:HIS73 2.4 13.4 0.6 CE1 A:HIS50 2.9 5.2 1.0 CD2 A:HIS73 2.9 12.2 0.4 HE1 A:HIS50 2.9 6.2 1.0 CE1 A:HIS48 2.9 5.6 1.0 HD2 A:HIS73 3.0 14.7 0.4 HE1 A:HIS48 3.0 6.7 1.0 CE1 A:HIS128 3.0 6.1 1.0 CD2 A:HIS73 3.1 12.3 0.6 HB2 A:HIS48 3.1 6.7 1.0 CE1 A:HIS73 3.1 10.6 0.4 HE1 A:HIS128 3.2 7.3 1.0 HD2 A:HIS73 3.2 14.8 0.6 CG A:HIS48 3.2 5.4 1.0 CD2 A:HIS128 3.2 5.7 1.0 O A:HOH562 3.3 6.6 0.4 CE1 A:HIS73 3.3 10.8 0.6 CD2 A:HIS50 3.3 5.2 1.0 HE1 A:HIS73 3.4 12.7 0.4 HD2 A:HIS128 3.5 6.8 1.0 HE1 A:HIS73 3.6 12.9 0.6 O A:HOH330 3.6 9.5 1.0 CB A:HIS48 3.6 5.5 1.0 HD2 A:HIS50 3.7 6.2 1.0 HB3 A:MET126 3.8 5.7 1.0 HG2 A:MET126 3.9 6.2 1.0 NE2 A:HIS48 4.0 5.4 1.0 ND1 A:HIS50 4.1 5.3 1.0 CG A:HIS73 4.1 8.4 0.4 CG A:HIS73 4.1 8.3 0.6 HB3 A:HIS48 4.1 6.7 1.0 ND1 A:HIS128 4.2 5.5 1.0 ND1 A:HIS73 4.2 7.3 0.4 CD2 A:HIS48 4.2 5.4 1.0 O A:HOH395 4.2 18.9 1.0 ND1 A:HIS73 4.2 7.3 0.6 CG A:HIS128 4.3 5.3 1.0 CG A:HIS50 4.3 5.2 1.0 CB A:MET126 4.5 4.8 1.0 CG A:MET126 4.6 5.1 1.0 HB2 A:MET126 4.8 5.7 1.0 HE2 A:HIS48 4.8 6.5 1.0 HD1 A:HIS50 4.8 6.3 1.0 HB3 A:LEU141 4.8 7.9 1.0 H A:HIS48 4.8 5.6 1.0 HG3 A:MET126 4.9 6.2 1.0 CA A:HIS48 4.9 5.0 1.0 HD1 A:HIS128 4.9 6.7 1.0

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.