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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

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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

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