Atomistry » Copper » PDB 4hhg-4m4l » 4l05
Atomistry »
  Copper »
    PDB 4hhg-4m4l »
      4l05 »

Copper 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:

Zinc (Zn) 1 atom

Copper Binding Sites:

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 4l05

Go back to Copper Binding Sites List in 4l05
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 4l05

Go back to Copper Binding Sites List in 4l05
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

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 Dec 13 11:15:09 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy