Manganese in PDB 6ghm: Structure of PP1 Alpha Phosphatase Bound to ASPP2

All present enzymatic activity of Structure of PP1 Alpha Phosphatase Bound to ASPP2:
3.1.3.16;

The structure of Structure of PP1 Alpha Phosphatase Bound to ASPP2, PDB code: 6ghm was solved by S.Mouilleron, T.M.Bertran, N.Tapon, Y.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.65 / 2.15
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	46.840, 81.624, 87.966, 91.06, 91.84, 103.89
R / Rfree (%)	17.7 / 21.5

The binding sites of Manganese atom in the Structure of PP1 Alpha Phosphatase Bound to ASPP2 (pdb code 6ghm). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Structure of PP1 Alpha Phosphatase Bound to ASPP2, PDB code: 6ghm:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Structure of PP1 Alpha Phosphatase Bound to ASPP2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of PP1 Alpha Phosphatase Bound to ASPP2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn412 b:32.9 occ:1.00 OD2 A:ASP92 2.1 33.5 1.0 OD2 A:ASP64 2.1 40.8 1.0 NE2 A:HIS66 2.2 39.7 1.0 O A:HOH501 2.2 32.2 1.0 O2 A:NHE411 2.3 44.8 0.5 O A:HOH551 2.4 41.8 1.0 CD2 A:HIS66 3.1 37.3 1.0 CG A:ASP92 3.1 31.3 1.0 MN A:MN413 3.2 26.8 1.0 CE1 A:HIS66 3.2 37.6 1.0 CG A:ASP64 3.3 32.8 1.0 O1 A:NHE411 3.3 37.1 0.5 S A:NHE411 3.3 40.3 0.5 CB A:ASP92 3.6 25.1 1.0 CB A:ASP64 4.1 31.4 1.0 C1 A:NHE411 4.1 32.9 0.5 C2 A:NHE411 4.2 38.5 0.5 OD1 A:ASP64 4.2 34.2 1.0 OD1 A:ASP92 4.2 32.2 1.0 NH2 A:ARG96 4.2 58.6 1.0 CG A:HIS66 4.3 39.5 1.0 ND1 A:HIS66 4.3 36.8 1.0 O A:HIS248 4.3 38.6 1.0 CD2 A:HIS125 4.4 37.3 1.0 OH A:TYR272 4.4 37.1 1.0 NE2 A:HIS173 4.5 28.9 1.0 CE1 A:HIS173 4.5 25.9 1.0 CE1 A:PHE267 4.5 32.2 1.0 NE2 A:HIS125 4.6 34.1 1.0 O3 A:NHE411 4.6 41.1 0.5 CA A:HIS248 4.6 29.1 1.0 C A:HIS248 4.7 31.4 1.0 OD1 A:ASN124 4.7 32.4 1.0 ND1 A:HIS248 4.8 32.7 1.0 N A:NHE411 5.0 32.5 0.5

Manganese binding site 2 out of 4 in the Structure of PP1 Alpha Phosphatase Bound to ASPP2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of PP1 Alpha Phosphatase Bound to ASPP2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn413 b:26.8 occ:1.00 O A:HOH501 1.8 32.2 1.0 OD1 A:ASN124 2.1 32.4 1.0 ND1 A:HIS248 2.1 32.7 1.0 NE2 A:HIS173 2.2 28.9 1.0 OD2 A:ASP92 2.3 33.5 1.0 O1 A:NHE411 2.5 37.1 0.5 CE1 A:HIS248 2.8 29.6 1.0 CG A:ASN124 3.1 31.0 1.0 CE1 A:HIS173 3.2 25.9 1.0 CD2 A:HIS173 3.2 22.5 1.0 CG A:ASP92 3.2 31.3 1.0 MN A:MN412 3.2 32.9 1.0 CG A:HIS248 3.3 30.1 1.0 OD1 A:ASP92 3.5 32.2 1.0 ND2 A:ASN124 3.6 30.3 1.0 S A:NHE411 3.7 40.3 0.5 CA A:HIS248 3.7 29.1 1.0 O2 A:NHE411 3.7 44.8 0.5 CB A:HIS248 3.9 29.3 1.0 O A:HIS248 4.0 38.6 1.0 OD2 A:ASP64 4.0 40.8 1.0 NE2 A:HIS248 4.1 29.6 1.0 ND1 A:HIS173 4.3 25.4 1.0 CD2 A:HIS248 4.3 29.4 1.0 CG A:HIS173 4.3 27.5 1.0 CD2 A:HIS125 4.4 37.3 1.0 C A:HIS248 4.4 31.4 1.0 CB A:ASN124 4.4 28.6 1.0 N A:ASN124 4.5 30.5 1.0 CB A:ASP92 4.5 25.1 1.0 O3 A:NHE411 4.5 41.1 0.5 O A:LEU205 4.6 32.2 1.0 N A:HIS248 4.8 29.8 1.0 NH1 A:ARG221 4.8 31.2 1.0 C1 A:NHE411 4.8 32.9 0.5 C2 A:NHE411 4.9 38.5 0.5 CG A:ASP64 4.9 32.8 1.0 CA A:ASN124 5.0 27.7 1.0 NE2 A:HIS66 5.0 39.7 1.0

Manganese binding site 3 out of 4 in the Structure of PP1 Alpha Phosphatase Bound to ASPP2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of PP1 Alpha Phosphatase Bound to ASPP2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn409 b:32.8 occ:1.00 OD2 B:ASP64 2.0 38.0 1.0 O B:HOH511 2.1 27.8 1.0 O B:HOH538 2.1 39.3 1.0 NE2 B:HIS66 2.2 41.5 1.0 OD2 B:ASP92 2.2 32.0 1.0 O3 B:NHE406 2.6 49.1 0.5 CE1 B:HIS66 3.1 39.0 1.0 CD2 B:HIS66 3.2 37.9 1.0 CG B:ASP64 3.2 32.3 1.0 CG B:ASP92 3.2 31.9 1.0 MN B:MN410 3.3 27.6 1.0 S B:NHE406 3.6 41.7 0.5 CB B:ASP92 3.7 23.0 1.0 O1 B:NHE406 3.8 31.4 0.5 CB B:ASP64 4.0 29.4 1.0 C2 B:NHE406 4.0 37.3 0.5 OD1 B:ASP64 4.1 33.0 1.0 O B:HIS248 4.2 31.6 1.0 ND1 B:HIS66 4.2 35.8 1.0 OH B:TYR272 4.3 42.5 1.0 OD1 B:ASP92 4.3 29.1 1.0 CG B:HIS66 4.3 37.3 1.0 C1 B:NHE406 4.3 42.5 0.5 CD2 B:HIS125 4.3 33.3 1.0 NE2 B:HIS125 4.4 36.8 1.0 NH1 B:ARG96 4.4 70.7 1.0 NE2 B:HIS173 4.4 34.2 1.0 CE1 B:PHE267 4.5 31.6 1.0 CE1 B:HIS173 4.5 31.0 1.0 CA B:HIS248 4.6 31.8 1.0 C B:HIS248 4.6 33.4 1.0 OD1 B:ASN124 4.8 29.1 1.0 N B:NHE406 4.8 39.6 0.5 ND1 B:HIS248 4.9 28.4 1.0 CZ B:TYR272 5.0 41.0 1.0

Manganese binding site 4 out of 4 in the Structure of PP1 Alpha Phosphatase Bound to ASPP2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of PP1 Alpha Phosphatase Bound to ASPP2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn410 b:27.6 occ:1.00 O B:HOH511 1.9 27.8 1.0 OD1 B:ASN124 2.0 29.1 1.0 NE2 B:HIS173 2.2 34.2 1.0 ND1 B:HIS248 2.2 28.4 1.0 OD2 B:ASP92 2.3 32.0 1.0 O1 B:NHE406 2.9 31.4 0.5 CE1 B:HIS248 2.9 25.2 1.0 CD2 B:HIS173 3.1 28.3 1.0 CG B:ASN124 3.1 31.3 1.0 CG B:ASP92 3.2 31.9 1.0 CE1 B:HIS173 3.2 31.0 1.0 MN B:MN409 3.3 32.8 1.0 CG B:HIS248 3.4 28.6 1.0 OD1 B:ASP92 3.4 29.1 1.0 CA B:HIS248 3.7 31.8 1.0 ND2 B:ASN124 3.8 27.4 1.0 S B:NHE406 3.9 41.7 0.5 CB B:HIS248 3.9 26.2 1.0 O3 B:NHE406 4.0 49.1 0.5 O B:HIS248 4.0 31.6 1.0 OD2 B:ASP64 4.1 38.0 1.0 NE2 B:HIS248 4.1 28.5 1.0 CD2 B:HIS125 4.2 33.3 1.0 ND1 B:HIS173 4.3 29.8 1.0 CG B:HIS173 4.3 30.5 1.0 C B:HIS248 4.3 33.4 1.0 CD2 B:HIS248 4.4 24.8 1.0 CB B:ASN124 4.4 31.4 1.0 C2 B:NHE406 4.4 37.3 0.5 N B:ASN124 4.4 31.1 1.0 CB B:ASP92 4.5 23.0 1.0 O B:LEU205 4.6 25.9 1.0 NE2 B:HIS125 4.7 36.8 1.0 N B:HIS248 4.7 28.7 1.0 CG B:ASP64 4.9 32.3 1.0 O B:HOH538 4.9 39.3 1.0 CA B:ASN124 4.9 33.9 1.0 OD1 B:ASP64 4.9 33.0 1.0

M.T.Bertran, S.Mouilleron, Y.Zhou, R.Bajaj, F.Uliana, G.S.Kumar, A.Van Drogen, R.Lee, J.J.Banerjee, S.Hauri, N.O'reilly, M.Gstaiger, R.Page, W.Peti, N.Tapon. Aspp Proteins Discriminate Between PP1 Catalytic Subunits Through Their SH3 Domain and the PP1 C-Tail. Nat Commun V. 10 771 2019.
ISSN: ESSN 2041-1723
PubMed: 30770806
DOI: 10.1038/S41467-019-08686-0