Manganese in PDB 3fga: Structural Basis of PP2A and Sgo Interaction

All present enzymatic activity of Structural Basis of PP2A and Sgo Interaction:
3.1.3.16;

The structure of Structural Basis of PP2A and Sgo Interaction, PDB code: 3fga was solved by Z.Xu, W.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.03 / 2.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	104.940, 145.856, 294.153, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 27.7

The binding sites of Manganese atom in the Structural Basis of PP2A and Sgo Interaction (pdb code 3fga). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structural Basis of PP2A and Sgo Interaction, PDB code: 3fga:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structural Basis of PP2A and Sgo Interaction


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structural Basis of PP2A and Sgo Interaction within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn311 b:48.9 occ:1.00 OD1 C:ASP57 2.2 28.9 1.0 NE2 C:HIS59 2.2 33.1 1.0 OD1 C:ASP85 2.3 33.8 1.0 CE1 C:HIS59 3.1 33.3 1.0 CG C:ASP57 3.2 30.1 1.0 MN C:MN312 3.3 26.4 1.0 CD2 C:HIS59 3.3 32.6 1.0 CG C:ASP85 3.5 35.2 1.0 O E:FGA6 3.7 96.8 1.0 O C:HOH355 3.7 22.0 1.0 OH C:TYR265 3.8 40.4 1.0 O C:HIS241 3.9 36.1 1.0 CB C:ASP57 4.0 30.4 1.0 NE2 C:HIS118 4.0 25.1 1.0 OD2 C:ASP57 4.1 32.0 1.0 CD2 C:HIS118 4.1 25.7 1.0 CB C:ASP85 4.1 34.9 1.0 ND1 C:HIS59 4.3 33.5 1.0 CE2 C:PHE260 4.3 31.9 1.0 CG C:HIS59 4.4 33.2 1.0 OD2 C:ASP85 4.4 36.1 1.0 CE1 C:HIS167 4.5 25.4 1.0 CZ C:TYR265 4.6 38.7 1.0 NE2 C:HIS167 4.7 25.4 1.0 C C:HIS241 4.7 36.2 1.0 ND2 C:ASN117 4.7 20.1 1.0 C E:FGA6 4.7 97.2 1.0 CZ C:PHE260 4.8 31.7 1.0 CE1 C:HIS118 4.8 22.6 1.0 ND1 C:HIS241 5.0 38.8 1.0 CG C:HIS118 5.0 26.2 1.0

Manganese binding site 2 out of 2 in the Structural Basis of PP2A and Sgo Interaction


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structural Basis of PP2A and Sgo Interaction within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn312 b:26.4 occ:1.00 ND2 C:ASN117 2.1 20.1 1.0 ND1 C:HIS241 2.1 38.8 1.0 NE2 C:HIS167 2.1 25.4 1.0 OD1 C:ASP85 2.5 33.8 1.0 CE1 C:HIS167 2.9 25.4 1.0 O C:HOH355 3.0 22.0 1.0 CG C:HIS241 3.0 37.0 1.0 CG C:ASN117 3.1 25.8 1.0 CE1 C:HIS241 3.1 37.5 1.0 CB C:HIS241 3.2 37.0 1.0 MN C:MN311 3.3 48.9 1.0 CD2 C:HIS167 3.3 27.7 1.0 CG C:ASP85 3.4 35.2 1.0 O C:HIS241 3.4 36.1 1.0 OD1 C:ASN117 3.4 26.5 1.0 OD2 C:ASP85 3.7 36.1 1.0 CA C:HIS241 3.8 36.6 1.0 OD1 C:ASP57 3.9 28.9 1.0 C C:HIS241 4.0 36.2 1.0 CD2 C:HIS118 4.1 25.7 1.0 ND1 C:HIS167 4.1 24.8 1.0 CD2 C:HIS241 4.1 36.4 1.0 NE2 C:HIS241 4.2 37.8 1.0 CG C:HIS167 4.3 27.9 1.0 CB C:ASN117 4.4 25.6 1.0 NE2 C:HIS118 4.5 25.1 1.0 OD2 C:ASP57 4.6 32.0 1.0 CG C:ASP57 4.6 30.1 1.0 CB C:ASP85 4.7 34.9 1.0 N C:ASN117 4.7 26.3 1.0 NH2 C:ARG214 4.8 42.1 1.0 O C:LEU199 4.9 31.1 1.0

Z.Xu, B.Cetin, M.Anger, U.S.Cho, W.Helmhart, K.Nasmyth, W.Xu. Structure and Function of the PP2A-Shugoshin Interaction Mol.Cell V. 35 426 2009.
ISSN: ISSN 1097-2765
PubMed: 19716788
DOI: 10.1016/J.MOLCEL.2009.06.031