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Manganese in PDB 2ce4: Manganese Superoxide Dismutase (Mn-Sod) From Deinococcus Radiodurans

Enzymatic activity of Manganese Superoxide Dismutase (Mn-Sod) From Deinococcus Radiodurans

All present enzymatic activity of Manganese Superoxide Dismutase (Mn-Sod) From Deinococcus Radiodurans:
1.15.1.1;

Protein crystallography data

The structure of Manganese Superoxide Dismutase (Mn-Sod) From Deinococcus Radiodurans, PDB code: 2ce4 was solved by R.Dennis, E.Micossi, J.Mccarthy, E.Moe, E.Gordon, G.Leonard, S.Mcsweeney, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.280, 83.210, 59.520, 90.00, 110.18, 90.00
R / Rfree (%) 16.8 / 23.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Manganese Superoxide Dismutase (Mn-Sod) From Deinococcus Radiodurans (pdb code 2ce4). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Manganese Superoxide Dismutase (Mn-Sod) From Deinococcus Radiodurans, PDB code: 2ce4:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2ce4

Go back to Manganese Binding Sites List in 2ce4
Manganese binding site 1 out of 2 in the Manganese Superoxide Dismutase (Mn-Sod) From Deinococcus Radiodurans


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 (Mn-Sod) From Deinococcus Radiodurans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1211

b:17.7
occ:1.00
OD2 A:ASP172 1.9 17.6 1.0
NE2 A:HIS80 2.0 18.2 1.0
O A:HOH2198 2.2 15.1 1.0
NE2 A:HIS176 2.2 20.8 1.0
NE2 A:HIS26 2.2 18.5 1.0
CE1 A:HIS80 3.0 20.0 1.0
CD2 A:HIS80 3.1 17.6 1.0
CG A:ASP172 3.1 19.2 1.0
CD2 A:HIS26 3.2 18.4 1.0
CD2 A:HIS176 3.2 20.8 1.0
CE1 A:HIS176 3.2 19.4 1.0
CE1 A:HIS26 3.2 18.9 1.0
OD1 A:ASP172 3.5 20.0 1.0
ND1 A:HIS80 4.1 20.9 1.0
CG A:HIS80 4.2 19.3 1.0
CB A:ASP172 4.3 19.9 1.0
ND1 A:HIS26 4.3 18.2 1.0
ND1 A:HIS176 4.3 19.1 1.0
CG A:HIS26 4.3 20.9 1.0
CG A:HIS176 4.3 19.8 1.0
CZ2 A:TRP133 4.4 18.2 1.0
NE2 A:GLN151 4.5 18.3 1.0
CB A:TRP174 4.6 16.3 1.0
CG A:TRP174 4.8 16.2 1.0
CB A:ALA177 4.9 17.7 1.0
CH2 A:TRP133 5.0 17.7 1.0

Manganese binding site 2 out of 2 in 2ce4

Go back to Manganese Binding Sites List in 2ce4
Manganese binding site 2 out of 2 in the Manganese Superoxide Dismutase (Mn-Sod) From Deinococcus Radiodurans


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 (Mn-Sod) From Deinococcus Radiodurans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1211

b:19.1
occ:1.00
OD2 B:ASP172 2.0 15.3 1.0
NE2 B:HIS176 2.1 18.5 1.0
NE2 B:HIS26 2.1 20.1 1.0
NE2 B:HIS80 2.2 23.8 1.0
O B:HOH2167 2.2 19.8 1.0
CE1 B:HIS176 3.1 20.9 1.0
CE1 B:HIS80 3.1 25.7 1.0
CG B:ASP172 3.1 18.3 1.0
CD2 B:HIS26 3.1 22.8 1.0
CD2 B:HIS176 3.1 18.8 1.0
CE1 B:HIS26 3.1 20.1 1.0
CD2 B:HIS80 3.2 25.6 1.0
OD1 B:ASP172 3.5 19.8 1.0
ND1 B:HIS176 4.2 19.8 1.0
ND1 B:HIS80 4.2 25.9 1.0
ND1 B:HIS26 4.2 17.4 1.0
CG B:HIS176 4.2 18.6 1.0
CG B:HIS26 4.2 22.0 1.0
CG B:HIS80 4.3 25.7 1.0
CB B:ASP172 4.4 18.6 1.0
CZ2 B:TRP133 4.5 18.7 1.0
NE2 B:GLN151 4.5 21.8 1.0
CB B:TRP174 4.6 17.6 1.0
CG B:TRP174 4.8 18.1 1.0
CB B:ALA177 4.9 18.9 1.0

Reference:

R.J.Dennis, E.Micossi, J.Mccarthy, E.Moe, E.J.Gordon, S.Kozielski-Stuhrmann, G.A.Leonard, S.Mcsweeney. Structure of the Manganese Superoxide Dismutase From Deinococcus Radiodurans in Two Crystal Forms. Acta Crystallogr. Sect. F V. 62 325 2006STRUCT. Biol. Cryst. Commun..
ISSN: ESSN 1744-3091
PubMed: 16582477
DOI: 10.1107/S1744309106008402
Page generated: Sat Oct 5 13:37:27 2024

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