Atomistry » Manganese » PDB 1lu1-1n0j » 1mng
Atomistry »
  Manganese »
    PDB 1lu1-1n0j »
      1mng »

Manganese in PDB 1mng: Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus

Enzymatic activity of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus

All present enzymatic activity of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus:
1.15.1.1;

Protein crystallography data

The structure of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus, PDB code: 1mng was solved by M.S.Lah, M.Dixon, K.A.Pattridge, W.C.Stallings, J.A.Fee, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 146.800, 146.800, 55.600, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / n/a

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus (pdb code 1mng). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus, PDB code: 1mng:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1mng

Go back to Manganese Binding Sites List in 1mng
Manganese binding site 1 out of 4 in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn204

b:8.1
occ:0.51
 MN A:MN204 0.0 8.1 0.5
MN A:MN204 0.4 7.3 0.5
O A:HOH207 2.0 6.0 0.5
NE2 A:HIS83 2.0 8.6 0.5
NE2 A:HIS170 2.0 7.9 0.5
NE2 A:HIS83 2.1 8.6 0.5
O A:HOH207 2.1 7.7 0.5
NE2 A:HIS170 2.1 7.9 0.5
OD2 A:ASP166 2.1 7.2 0.5
NE2 A:HIS28 2.2 6.5 0.5
OD2 A:ASP166 2.2 7.1 0.5
NE2 A:HIS28 2.2 6.3 0.5
N1 A:AZI206 2.3 9.9 0.5
CE1 A:HIS170 2.9 7.3 0.5
CE1 A:HIS83 3.0 8.2 0.5
CE1 A:HIS83 3.1 8.7 0.5
CD2 A:HIS83 3.1 8.9 0.5
CE1 A:HIS170 3.1 7.1 0.5
CD2 A:HIS170 3.1 7.2 0.5
CD2 A:HIS83 3.1 9.2 0.5
CD2 A:HIS28 3.1 5.6 0.5
CD2 A:HIS170 3.1 6.9 0.5
CD2 A:HIS28 3.2 5.8 0.5
CE1 A:HIS28 3.2 5.6 0.5
CG A:ASP166 3.2 7.6 0.5
CG A:ASP166 3.2 7.1 0.5
CE1 A:HIS28 3.3 5.2 0.5
N2 A:AZI206 3.3 13.0 0.5
OD1 A:ASP166 3.6 8.4 0.5
OD1 A:ASP166 3.6 7.3 0.5
ND1 A:HIS170 4.1 7.3 0.5
ND1 A:HIS83 4.1 7.5 0.5
CG A:HIS170 4.2 7.0 0.5
CG A:HIS83 4.2 8.4 0.5
ND1 A:HIS83 4.2 7.9 0.5
ND1 A:HIS170 4.2 7.8 0.5
CG A:HIS83 4.3 8.7 0.5
CG A:HIS170 4.3 7.2 0.5
ND1 A:HIS28 4.3 6.2 0.5
CG A:HIS28 4.3 6.3 0.5
CG A:HIS28 4.3 6.6 0.5
ND1 A:HIS28 4.3 6.0 0.5
CZ2 A:TRP132 4.4 5.0 1.0
N3 A:AZI206 4.4 15.3 0.5
CB A:ASP166 4.4 7.3 0.5
NE2 A:GLN151 4.5 6.1 1.0
CB A:ASP166 4.5 7.5 0.5
CB A:TRP168 4.7 6.8 1.0
CG A:TRP168 4.9 5.5 1.0

Manganese binding site 2 out of 4 in 1mng

Go back to Manganese Binding Sites List in 1mng
Manganese binding site 2 out of 4 in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn204

b:7.3
occ:0.52
 MN A:MN204 0.0 7.3 0.5
MN A:MN204 0.4 8.1 0.5
OD2 A:ASP166 1.7 7.2 0.5
OD2 A:ASP166 1.8 7.1 0.5
O A:HOH207 2.0 6.0 0.5
O A:HOH207 2.1 7.7 0.5
NE2 A:HIS83 2.1 8.6 0.5
NE2 A:HIS28 2.1 6.3 0.5
NE2 A:HIS28 2.1 6.5 0.5
NE2 A:HIS170 2.2 7.9 0.5
NE2 A:HIS83 2.2 8.6 0.5
NE2 A:HIS170 2.3 7.9 0.5
N1 A:AZI206 2.7 9.9 0.5
CG A:ASP166 2.8 7.6 0.5
CG A:ASP166 2.9 7.1 0.5
CE1 A:HIS28 3.0 5.6 0.5
CE1 A:HIS28 3.1 5.2 0.5
CE1 A:HIS83 3.1 8.2 0.5
CD2 A:HIS83 3.1 8.9 0.5
CD2 A:HIS170 3.2 7.2 0.5
CE1 A:HIS170 3.2 7.3 0.5
CD2 A:HIS83 3.2 9.2 0.5
CD2 A:HIS28 3.2 5.6 0.5
CD2 A:HIS170 3.2 6.9 0.5
CD2 A:HIS28 3.3 5.8 0.5
CE1 A:HIS83 3.3 8.7 0.5
CE1 A:HIS170 3.3 7.1 0.5
OD1 A:ASP166 3.3 8.4 0.5
OD1 A:ASP166 3.3 7.3 0.5
N2 A:AZI206 3.7 13.0 0.5
CB A:ASP166 4.1 7.3 0.5
CB A:ASP166 4.1 7.5 0.5
CZ2 A:TRP132 4.2 5.0 1.0
ND1 A:HIS28 4.2 6.2 0.5
ND1 A:HIS28 4.2 6.0 0.5
ND1 A:HIS83 4.2 7.5 0.5
CG A:HIS83 4.3 8.4 0.5
ND1 A:HIS170 4.3 7.3 0.5
CG A:HIS170 4.3 7.0 0.5
CG A:HIS28 4.3 6.3 0.5
CG A:HIS28 4.3 6.6 0.5
CG A:HIS83 4.4 8.7 0.5
ND1 A:HIS83 4.4 7.9 0.5
ND1 A:HIS170 4.4 7.8 0.5
CG A:HIS170 4.4 7.2 0.5
NE2 A:GLN151 4.7 6.1 1.0
CB A:TRP168 4.7 6.8 1.0
N3 A:AZI206 4.7 15.3 0.5
CG A:TRP168 4.9 5.5 1.0
CB A:ALA171 4.9 6.1 1.0
CH2 A:TRP132 4.9 3.8 1.0
CE2 A:TRP132 4.9 6.0 1.0

Manganese binding site 3 out of 4 in 1mng

Go back to Manganese Binding Sites List in 1mng
Manganese binding site 3 out of 4 in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn204

b:8.8
occ:0.50
 MN B:MN204 0.0 8.8 0.5
MN B:MN204 0.4 7.4 0.6
O B:HOH207 1.9 9.4 0.5
NE2 B:HIS170 2.0 9.0 0.6
NE2 B:HIS83 2.0 7.9 0.6
NE2 B:HIS83 2.0 9.3 0.5
NE2 B:HIS28 2.1 7.6 0.5
NE2 B:HIS170 2.1 10.2 0.5
N1 B:AZI206 2.1 12.1 0.5
O B:HOH207 2.1 7.5 0.6
OD2 B:ASP166 2.2 8.8 0.5
OD2 B:ASP166 2.2 7.0 0.6
NE2 B:HIS28 2.2 6.3 0.6
CE1 B:HIS170 2.9 8.3 0.6
CE1 B:HIS83 3.0 7.8 0.6
CE1 B:HIS83 3.0 8.7 0.5
CE1 B:HIS28 3.0 6.7 0.5
CD2 B:HIS170 3.1 8.5 0.6
CE1 B:HIS170 3.1 9.3 0.5
CD2 B:HIS28 3.1 6.8 0.5
CD2 B:HIS28 3.1 6.2 0.6
CD2 B:HIS83 3.1 6.7 0.6
CD2 B:HIS83 3.2 7.5 0.5
CD2 B:HIS170 3.2 9.2 0.5
N2 B:AZI206 3.2 14.9 0.5
CG B:ASP166 3.2 6.7 0.6
CG B:ASP166 3.2 8.0 0.5
CE1 B:HIS28 3.2 6.2 0.6
OD1 B:ASP166 3.5 7.0 0.6
OD1 B:ASP166 3.5 8.3 0.5
ND1 B:HIS170 4.1 8.9 0.6
ND1 B:HIS83 4.1 8.0 0.6
ND1 B:HIS83 4.1 8.6 0.5
ND1 B:HIS28 4.2 6.5 0.5
CG B:HIS170 4.2 8.4 0.6
CG B:HIS28 4.2 7.3 0.5
ND1 B:HIS170 4.2 9.8 0.5
CG B:HIS83 4.2 7.1 0.6
CG B:HIS83 4.3 7.8 0.5
CG B:HIS28 4.3 7.0 0.6
CG B:HIS170 4.3 9.1 0.5
N3 B:AZI206 4.3 16.6 0.5
ND1 B:HIS28 4.3 6.9 0.6
CZ2 B:TRP132 4.4 5.7 1.0
NE2 B:GLN151 4.4 5.2 1.0
CB B:ASP166 4.5 8.2 0.5
CB B:ASP166 4.5 7.7 0.6
CB B:TRP168 4.7 3.7 1.0
CG B:TRP168 4.8 4.6 1.0

Manganese binding site 4 out of 4 in 1mng

Go back to Manganese Binding Sites List in 1mng
Manganese binding site 4 out of 4 in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn204

b:7.4
occ:0.55
 MN B:MN204 0.0 7.4 0.6
MN B:MN204 0.4 8.8 0.5
OD2 B:ASP166 1.8 8.8 0.5
OD2 B:ASP166 1.8 7.0 0.6
O B:HOH207 2.0 9.4 0.5
NE2 B:HIS28 2.0 7.6 0.5
NE2 B:HIS83 2.1 7.9 0.6
O B:HOH207 2.1 7.5 0.6
NE2 B:HIS83 2.1 9.3 0.5
NE2 B:HIS28 2.1 6.3 0.6
NE2 B:HIS170 2.2 9.0 0.6
NE2 B:HIS170 2.3 10.2 0.5
N1 B:AZI206 2.5 12.1 0.5
CG B:ASP166 2.8 6.7 0.6
CG B:ASP166 2.8 8.0 0.5
CE1 B:HIS28 2.8 6.7 0.5
CE1 B:HIS28 3.1 6.2 0.6
CE1 B:HIS83 3.1 7.8 0.6
CE1 B:HIS83 3.1 8.7 0.5
CD2 B:HIS83 3.1 6.7 0.6
CD2 B:HIS83 3.2 7.5 0.5
CD2 B:HIS28 3.2 6.2 0.6
CD2 B:HIS28 3.2 6.8 0.5
CD2 B:HIS170 3.2 8.5 0.6
CE1 B:HIS170 3.2 8.3 0.6
OD1 B:ASP166 3.2 7.0 0.6
OD1 B:ASP166 3.3 8.3 0.5
CD2 B:HIS170 3.3 9.2 0.5
CE1 B:HIS170 3.3 9.3 0.5
N2 B:AZI206 3.6 14.9 0.5
ND1 B:HIS28 4.1 6.5 0.5
CB B:ASP166 4.1 8.2 0.5
CB B:ASP166 4.1 7.7 0.6
CZ2 B:TRP132 4.2 5.7 1.0
ND1 B:HIS28 4.2 6.9 0.6
ND1 B:HIS83 4.2 8.0 0.6
ND1 B:HIS83 4.2 8.6 0.5
CG B:HIS28 4.2 7.3 0.5
CG B:HIS83 4.3 7.1 0.6
CG B:HIS83 4.3 7.8 0.5
CG B:HIS28 4.3 7.0 0.6
ND1 B:HIS170 4.3 8.9 0.6
CG B:HIS170 4.4 8.4 0.6
ND1 B:HIS170 4.5 9.8 0.5
CG B:HIS170 4.5 9.1 0.5
NE2 B:GLN151 4.6 5.2 1.0
CB B:TRP168 4.7 3.7 1.0
N3 B:AZI206 4.7 16.6 0.5
CG B:TRP168 4.8 4.6 1.0
CH2 B:TRP132 4.9 5.5 1.0
CB B:ALA171 4.9 7.3 1.0
CE2 B:TRP132 4.9 4.4 1.0

Reference:

M.S.Lah, M.M.Dixon, K.A.Pattridge, W.C.Stallings, J.A.Fee, M.L.Ludwig. Structure-Function in Escherichia Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From Thermus Thermophilus. Biochemistry V. 34 1646 1995.
ISSN: ISSN 0006-2960
PubMed: 7849024
DOI: 10.1021/BI00005A021
Page generated: Sat Oct 5 11:43:43 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy