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Manganese in PDB 1gv3: The 2.0 Angstrom Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase

Protein crystallography data

The structure of The 2.0 Angstrom Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase, PDB code: 1gv3 was solved by W.Atzenhofer, G.Regelsberger, U.Jacob, R.Huber, G.A.Peschek, C.Obinger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.00
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 151.320, 151.320, 69.280, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 21.1

Manganese Binding Sites:

The binding sites of Manganese atom in the The 2.0 Angstrom Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase (pdb code 1gv3). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The 2.0 Angstrom Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase, PDB code: 1gv3:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1gv3

Go back to Manganese Binding Sites List in 1gv3
Manganese binding site 1 out of 2 in the The 2.0 Angstrom Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The 2.0 Angstrom Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1238

b:8.0
occ:0.52
OD2 A:ASP200 2.0 20.2 1.0
O A:HOH2079 2.1 1.9 0.5
NE2 A:HIS117 2.2 21.4 1.0
NE2 A:HIS62 2.2 18.8 1.0
NE2 A:HIS204 2.2 22.4 1.0
CE1 A:HIS117 3.0 21.7 1.0
CG A:ASP200 3.1 19.9 1.0
CE1 A:HIS204 3.1 21.5 1.0
CD2 A:HIS62 3.2 18.7 1.0
CE1 A:HIS62 3.2 19.2 1.0
CD2 A:HIS204 3.3 22.1 1.0
CD2 A:HIS117 3.3 21.9 1.0
OD1 A:ASP200 3.6 23.1 1.0
ND1 A:HIS117 4.2 18.8 1.0
ND1 A:HIS204 4.3 21.1 1.0
ND1 A:HIS62 4.3 17.4 1.0
CG A:HIS62 4.3 17.8 1.0
CG A:HIS117 4.3 23.3 1.0
CB A:ASP200 4.4 15.8 1.0
CG A:HIS204 4.4 20.7 1.0
CZ2 A:TRP166 4.5 21.8 1.0
NE2 A:GLN185 4.5 18.3 1.0
CB A:TRP202 4.6 15.1 1.0
CG A:TRP202 4.7 16.4 1.0
CB A:ALA205 5.0 21.4 1.0
CD1 A:TRP202 5.0 14.8 1.0

Manganese binding site 2 out of 2 in 1gv3

Go back to Manganese Binding Sites List in 1gv3
Manganese binding site 2 out of 2 in the The 2.0 Angstrom Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The 2.0 Angstrom Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1238

b:10.1
occ:0.55
OD2 B:ASP200 2.0 19.5 1.0
O B:HOH2087 2.1 7.9 0.6
NE2 B:HIS62 2.2 19.6 1.0
NE2 B:HIS204 2.2 22.7 1.0
NE2 B:HIS117 2.2 20.8 1.0
CE1 B:HIS62 3.1 20.4 1.0
CE1 B:HIS117 3.1 20.3 1.0
CG B:ASP200 3.1 18.8 1.0
CE1 B:HIS204 3.1 20.9 1.0
CD2 B:HIS62 3.2 18.1 1.0
CD2 B:HIS204 3.2 21.4 1.0
CD2 B:HIS117 3.2 18.5 1.0
OD1 B:ASP200 3.6 20.0 1.0
ND1 B:HIS62 4.2 17.2 1.0
ND1 B:HIS204 4.3 22.0 1.0
ND1 B:HIS117 4.3 18.7 1.0
CG B:HIS62 4.3 19.1 1.0
CG B:HIS204 4.3 19.5 1.0
CB B:ASP200 4.3 19.0 1.0
CG B:HIS117 4.3 20.8 1.0
CZ2 B:TRP166 4.3 17.9 1.0
NE2 B:GLN185 4.5 15.0 1.0
CB B:TRP202 4.6 16.0 1.0
CG B:TRP202 4.8 16.1 1.0
CB B:ALA205 5.0 17.7 1.0

Reference:

W.Atzenhofer, G.Regelsberger, U.Jacob, G.A.Peschek, P.Furtmuller, R.Huber, C.Obinger. The 2.0A Resolution Structure of the Catalytic Portion of A Cyanobacterial Membrane-Bound Manganese Superoxide Dismutase J.Mol.Biol. V. 321 479 2002.
ISSN: ISSN 0022-2836
PubMed: 12162960
DOI: 10.1016/S0022-2836(02)00624-1
Page generated: Tue Dec 15 03:48:35 2020

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