Manganese in PDB 4lac: Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas

All present enzymatic activity of Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas:
3.1.3.16; 5.2.1.8;

The structure of Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas, PDB code: 4lac was solved by F.Guo, V.Stanevich, N.Wlodarchak, K.A.Satyshur, Y.Xing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.82
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.070, 100.186, 167.450, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 24.2

The binding sites of Manganese atom in the Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas (pdb code 4lac). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas, PDB code: 4lac:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn501 b:25.6 occ:1.00 NE2 C:HIS167 2.1 25.0 1.0 OD1 C:ASN117 2.1 26.7 1.0 OD2 C:ASP85 2.3 26.4 1.0 ND1 C:HIS241 2.3 25.2 1.0 O2G C:AGS503 2.3 31.7 1.0 CE1 C:HIS241 3.0 25.4 1.0 CE1 C:HIS167 3.0 25.0 1.0 S1G C:AGS503 3.1 36.0 1.0 CG C:ASP85 3.1 26.4 1.0 CD2 C:HIS167 3.2 25.0 1.0 CG C:ASN117 3.2 26.8 1.0 PG C:AGS503 3.2 32.9 1.0 OD1 C:ASP85 3.3 26.3 1.0 MN C:MN502 3.5 35.0 1.0 CG C:HIS241 3.5 25.2 1.0 ND2 C:ASN117 3.6 26.9 1.0 CA C:HIS241 3.8 24.8 1.0 CB C:HIS241 4.0 25.0 1.0 CD2 C:HIS118 4.1 27.7 1.0 ND1 C:HIS167 4.2 24.8 1.0 NE2 C:HIS241 4.2 25.6 1.0 OD2 C:ASP57 4.3 28.2 1.0 O3G C:AGS503 4.3 32.7 1.0 O C:HIS241 4.3 25.9 1.0 CG C:HIS167 4.3 24.8 1.0 CB C:ASP85 4.4 26.5 1.0 O3B C:AGS503 4.4 34.4 1.0 C C:HIS241 4.5 25.5 1.0 CD2 C:HIS241 4.5 25.4 1.0 CB C:ASN117 4.5 26.5 1.0 N C:ASN117 4.6 26.4 1.0 N C:HIS241 4.7 24.4 1.0 NE2 C:HIS118 4.8 28.3 1.0 O C:LEU199 4.9 24.6 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Protein Phosphatase 2A (PP2A) and PP2A Phosphatase Activator (Ptpa) Complex with Atpgammas within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn502 b:35.0 occ:1.00 NE2 C:HIS59 2.0 27.2 1.0 OD2 C:ASP57 2.1 28.2 1.0 OD2 C:ASP85 2.2 26.4 1.0 S1G C:AGS503 2.3 36.0 1.0 CE1 C:HIS59 2.8 27.2 1.0 O3G C:AGS503 3.1 32.7 1.0 CD2 C:HIS59 3.1 27.4 1.0 PG C:AGS503 3.2 32.9 1.0 CG C:ASP57 3.3 27.8 1.0 CG C:ASP85 3.3 26.4 1.0 MN C:MN501 3.5 25.6 1.0 CB C:ASP85 3.7 26.5 1.0 O2G C:AGS503 3.7 31.7 1.0 ND1 C:HIS59 4.0 27.2 1.0 CB C:ASP57 4.1 27.5 1.0 CD2 C:HIS118 4.2 27.7 1.0 CG C:HIS59 4.2 27.3 1.0 OD1 C:ASP57 4.2 27.4 1.0 NH1 C:ARG89 4.4 27.4 1.0 NE2 C:HIS118 4.4 28.3 1.0 OD1 C:ASP85 4.4 26.3 1.0 CE1 C:HIS167 4.6 25.0 1.0 O3B C:AGS503 4.7 34.4 1.0 CE1 C:PHE260 4.7 24.1 1.0 NE2 C:HIS167 4.7 25.0 1.0 CA C:HIS241 4.9 24.8 1.0 O C:HIS241 4.9 25.9 1.0 C C:HIS241 4.9 25.5 1.0

F.Guo, V.Stanevich, N.Wlodarchak, R.Sengupta, L.Jiang, K.A.Satyshur, Y.Xing. Structural Basis of PP2A Activation By Ptpa, An Atp-Dependent Activation Chaperone. Cell Res. V. 24 190 2014.
ISSN: ISSN 1001-0602
PubMed: 24100351
DOI: 10.1038/CR.2013.138