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Manganese in PDB 1vew: Manganese Superoxide Dismutase From Escherichia Coli

Enzymatic activity of Manganese Superoxide Dismutase From Escherichia Coli

All present enzymatic activity of Manganese Superoxide Dismutase From Escherichia Coli:
1.15.1.1;

Protein crystallography data

The structure of Manganese Superoxide Dismutase From Escherichia Coli, PDB code: 1vew was solved by R.A.Edwards, H.M.Baker, M.M.Whittaker, J.W.Whittaker, G.B.Jameson, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 100.840, 108.910, 182.100, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 21.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Manganese Superoxide Dismutase From Escherichia Coli (pdb code 1vew). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Manganese Superoxide Dismutase From Escherichia Coli, PDB code: 1vew:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 1vew

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Manganese binding site 1 out of 4 in the Manganese Superoxide Dismutase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Manganese Superoxide Dismutase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn206

b:20.7
occ:1.00
OD2 A:ASP167 2.0 23.0 1.0
NE2 A:HIS26 2.1 21.0 1.0
O A:OH207 2.2 16.7 1.0
NE2 A:HIS171 2.2 17.8 1.0
NE2 A:HIS81 2.2 22.1 1.0
CE1 A:HIS26 3.1 20.8 1.0
CG A:ASP167 3.1 26.4 1.0
CD2 A:HIS171 3.1 17.8 1.0
CE1 A:HIS81 3.1 22.2 1.0
CD2 A:HIS26 3.2 21.2 1.0
CE1 A:HIS171 3.2 17.8 1.0
CD2 A:HIS81 3.2 22.1 1.0
OD1 A:ASP167 3.5 22.9 1.0
ND1 A:HIS26 4.2 21.8 1.0
ND1 A:HIS81 4.3 22.2 1.0
CG A:HIS171 4.3 17.3 1.0
ND1 A:HIS171 4.3 18.1 1.0
CG A:HIS26 4.3 20.5 1.0
CG A:HIS81 4.3 21.2 1.0
CB A:ASP167 4.4 19.2 1.0
CZ2 A:TRP128 4.5 24.6 1.0
NE2 A:GLN146 4.6 17.6 1.0
CB A:TRP169 4.7 17.3 1.0
CG A:TRP169 4.8 18.2 1.0
CB A:ALA172 4.9 17.8 1.0
CH2 A:TRP128 5.0 25.2 1.0

Manganese binding site 2 out of 4 in 1vew

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Manganese binding site 2 out of 4 in the Manganese Superoxide Dismutase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Manganese Superoxide Dismutase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn206

b:22.5
occ:1.00
OD2 B:ASP167 2.0 24.3 1.0
NE2 B:HIS26 2.1 21.2 1.0
NE2 B:HIS171 2.2 17.9 1.0
O B:OH207 2.2 15.6 1.0
NE2 B:HIS81 2.2 22.6 1.0
CE1 B:HIS26 3.0 21.0 1.0
CD2 B:HIS171 3.1 17.8 1.0
CD2 B:HIS26 3.1 21.8 1.0
CG B:ASP167 3.1 26.8 1.0
CE1 B:HIS81 3.2 22.2 1.0
CD2 B:HIS81 3.2 22.4 1.0
CE1 B:HIS171 3.2 17.9 1.0
OD1 B:ASP167 3.5 23.2 1.0
ND1 B:HIS26 4.2 21.8 1.0
CG B:HIS26 4.2 20.6 1.0
CG B:HIS171 4.3 17.5 1.0
ND1 B:HIS171 4.3 18.2 1.0
ND1 B:HIS81 4.3 22.7 1.0
CG B:HIS81 4.3 21.3 1.0
CB B:ASP167 4.4 19.3 1.0
CZ2 B:TRP128 4.5 25.1 1.0
CB B:TRP169 4.7 17.6 1.0
NE2 B:GLN146 4.7 18.1 1.0
CG B:TRP169 4.9 18.2 1.0
CB B:ALA172 4.9 17.5 1.0

Manganese binding site 3 out of 4 in 1vew

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Manganese binding site 3 out of 4 in the Manganese Superoxide Dismutase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Manganese Superoxide Dismutase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn206

b:22.4
occ:1.00
OD2 C:ASP167 2.0 23.6 1.0
NE2 C:HIS171 2.2 17.2 1.0
NE2 C:HIS26 2.2 20.9 1.0
NE2 C:HIS81 2.2 22.7 1.0
O C:OH207 2.3 15.0 1.0
CG C:ASP167 3.1 26.3 1.0
CD2 C:HIS171 3.1 17.8 1.0
CE1 C:HIS26 3.1 20.5 1.0
CE1 C:HIS81 3.1 22.2 1.0
CE1 C:HIS171 3.2 17.6 1.0
CD2 C:HIS26 3.2 21.0 1.0
CD2 C:HIS81 3.2 22.5 1.0
OD1 C:ASP167 3.5 22.7 1.0
ND1 C:HIS26 4.3 21.4 1.0
ND1 C:HIS171 4.3 18.5 1.0
ND1 C:HIS81 4.3 22.1 1.0
CG C:HIS171 4.3 17.7 1.0
CG C:HIS26 4.3 20.6 1.0
CG C:HIS81 4.3 21.5 1.0
CB C:ASP167 4.4 18.8 1.0
CZ2 C:TRP128 4.5 24.7 1.0
NE2 C:GLN146 4.6 18.4 1.0
CB C:TRP169 4.7 17.6 1.0
CG C:TRP169 4.9 18.0 1.0
CB C:ALA172 4.9 17.8 1.0
CH2 C:TRP128 5.0 25.7 1.0

Manganese binding site 4 out of 4 in 1vew

Go back to Manganese Binding Sites List in 1vew
Manganese binding site 4 out of 4 in the Manganese Superoxide Dismutase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Manganese Superoxide Dismutase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn206

b:21.5
occ:1.00
OD2 D:ASP167 2.0 23.6 1.0
NE2 D:HIS26 2.1 20.6 1.0
NE2 D:HIS171 2.2 17.2 1.0
O D:OH207 2.2 19.0 1.0
NE2 D:HIS81 2.2 22.6 1.0
CE1 D:HIS26 3.1 20.7 1.0
CG D:ASP167 3.1 26.5 1.0
CD2 D:HIS171 3.1 17.8 1.0
CD2 D:HIS26 3.1 21.1 1.0
CE1 D:HIS81 3.2 22.4 1.0
CE1 D:HIS171 3.2 17.7 1.0
CD2 D:HIS81 3.2 22.3 1.0
OD1 D:ASP167 3.5 22.9 1.0
ND1 D:HIS26 4.2 21.6 1.0
CG D:HIS26 4.3 20.6 1.0
CG D:HIS171 4.3 17.4 1.0
ND1 D:HIS81 4.3 22.4 1.0
ND1 D:HIS171 4.3 18.0 1.0
CG D:HIS81 4.3 21.2 1.0
CB D:ASP167 4.4 19.6 1.0
CZ2 D:TRP128 4.5 24.8 1.0
NE2 D:GLN146 4.6 18.4 1.0
CB D:TRP169 4.7 17.6 1.0
CG D:TRP169 4.8 18.5 1.0
CB D:ALA172 4.9 18.1 1.0

Reference:

R.A.Edwards, H.M.Baker, M.M.Whittaker, J.W.Whittaker, G.B.Jameson, E.N.Baker. Crystal Structure of Escherichia Coli Manganese Superoxide Dismutase at 2.1-Angstrom Resolution. J.Biol.Inorg.Chem. V. 3 161 1998.
ISSN: ISSN 0949-8257
Page generated: Tue Dec 15 03:57:00 2020

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