Manganese in PDB 4mov: 1.45 A Resolution Crystal Structure of Protein Phosphatase 1

All present enzymatic activity of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1:
3.1.3.16;

The structure of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1, PDB code: 4mov was solved by M.S.Choy, W.Peti, R.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.93 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.724, 77.600, 133.035, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 16.7

The structure of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Manganese atom in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 (pdb code 4mov). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1, PDB code: 4mov:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:9.0 occ:1.00 OD1 A:ASN124 2.1 7.9 1.0 O3 A:PO4403 2.2 11.4 0.8 NE2 A:HIS173 2.2 7.7 1.0 OD2 A:ASP92 2.2 8.2 1.0 ND1 A:HIS248 2.2 10.6 1.0 O A:HOH737 2.3 13.0 1.0 CE1 A:HIS248 3.1 11.6 1.0 MN A:MN402 3.1 13.4 0.5 CG A:ASP92 3.2 7.8 1.0 CE1 A:HIS173 3.2 7.3 1.0 CG A:ASN124 3.2 9.2 1.0 CD2 A:HIS173 3.2 6.5 1.0 CG A:HIS248 3.4 9.0 1.0 P A:PO4403 3.4 17.4 0.8 OD1 A:ASP92 3.5 7.5 1.0 ND2 A:ASN124 3.6 10.9 1.0 O1 A:PO4403 3.7 19.6 0.8 CA A:HIS248 3.8 9.9 1.0 CB A:HIS248 3.9 9.5 1.0 OD2 A:ASP64 4.0 11.8 1.0 O4 A:PO4403 4.1 19.7 0.8 O A:HIS248 4.1 17.6 1.0 CD2 A:HIS125 4.2 9.3 1.0 NE2 A:HIS248 4.3 13.5 1.0 ND1 A:HIS173 4.3 6.9 1.0 CG A:HIS173 4.3 7.1 1.0 CD2 A:HIS248 4.4 14.3 1.0 CB A:ASP92 4.4 6.9 1.0 CB A:ASN124 4.5 8.6 1.0 C A:HIS248 4.5 12.0 1.0 N A:ASN124 4.5 7.5 1.0 O2 A:PO4403 4.6 18.8 0.8 O A:LEU205 4.7 10.1 1.0 NE2 A:HIS125 4.8 9.8 1.0 N A:HIS248 4.9 9.5 1.0 NE2 A:HIS66 4.9 9.6 1.0 O A:HOH746 4.9 33.5 1.0 CG A:ASP64 4.9 9.8 1.0

Manganese binding site 2 out of 4 in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:13.4 occ:0.50 O A:HOH737 1.7 13.0 1.0 NE2 A:HIS66 2.1 9.6 1.0 OD2 A:ASP92 2.2 8.2 1.0 O1 A:PO4403 2.2 19.6 0.8 O A:HOH746 2.3 33.5 1.0 OD2 A:ASP64 2.3 11.8 1.0 CE1 A:HIS66 3.0 8.4 1.0 CD2 A:HIS66 3.1 9.2 1.0 MN A:MN401 3.1 9.0 1.0 CG A:ASP92 3.3 7.8 1.0 P A:PO4403 3.3 17.4 0.8 O3 A:PO4403 3.4 11.4 0.8 CG A:ASP64 3.5 9.8 1.0 CB A:ASP92 3.7 6.9 1.0 O A:HIS248 4.0 17.6 1.0 O A:HOH791 4.0 38.9 1.0 O4 A:PO4403 4.1 19.7 0.8 ND1 A:HIS66 4.2 7.5 1.0 CB A:ASP64 4.2 8.1 1.0 NH1 A:ARG96 4.2 21.1 1.0 CG A:HIS66 4.2 6.9 1.0 CD2 A:HIS125 4.3 9.3 1.0 CE2 A:PHE267 4.3 8.9 1.0 OD1 A:ASP92 4.4 7.5 1.0 NE2 A:HIS173 4.4 7.7 1.0 OD1 A:ASP64 4.5 9.7 1.0 CE1 A:HIS173 4.5 7.3 1.0 OH A:TYR272 4.5 26.7 1.0 NE2 A:HIS125 4.5 9.8 1.0 O2 A:PO4403 4.6 18.8 0.8 CA A:HIS248 4.6 9.9 1.0 C A:HIS248 4.7 12.0 1.0 ND1 A:HIS248 4.7 10.6 1.0 OD1 A:ASN124 4.9 7.9 1.0 CZ A:PHE267 4.9 11.7 1.0

Manganese binding site 3 out of 4 in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:9.8 occ:1.00 OD1 B:ASN124 2.1 10.4 1.0 O1 B:PO4403 2.2 11.7 0.8 OD2 B:ASP92 2.2 9.3 1.0 NE2 B:HIS173 2.2 9.6 1.0 ND1 B:HIS248 2.2 10.6 1.0 O B:HOH508 2.3 13.6 1.0 CE1 B:HIS248 3.1 11.5 1.0 CG B:ASP92 3.2 9.5 1.0 CG B:ASN124 3.2 10.0 1.0 CE1 B:HIS173 3.2 10.2 1.0 MN B:MN402 3.2 13.6 0.5 CD2 B:HIS173 3.2 9.8 1.0 CG B:HIS248 3.4 10.6 1.0 P B:PO4403 3.4 18.5 0.8 OD1 B:ASP92 3.5 9.4 1.0 ND2 B:ASN124 3.6 11.3 1.0 O3 B:PO4403 3.7 20.3 0.8 CA B:HIS248 3.8 11.0 1.0 CB B:HIS248 3.9 10.0 1.0 OD2 B:ASP64 3.9 13.2 1.0 O2 B:PO4403 4.1 21.7 0.8 O B:HIS248 4.1 20.6 1.0 CD2 B:HIS125 4.2 9.8 1.0 NE2 B:HIS248 4.2 12.6 1.0 ND1 B:HIS173 4.3 8.4 1.0 CG B:HIS173 4.4 8.0 1.0 CB B:ASP92 4.4 8.1 1.0 CD2 B:HIS248 4.4 13.3 1.0 C B:HIS248 4.5 13.6 1.0 CB B:ASN124 4.5 9.7 1.0 N B:ASN124 4.5 8.7 1.0 O4 B:PO4403 4.6 20.1 0.8 O B:LEU205 4.7 12.1 1.0 NE2 B:HIS125 4.8 10.9 1.0 N B:HIS248 4.9 10.1 1.0 CG B:ASP64 4.9 9.3 1.0 NE2 B:HIS66 4.9 10.6 1.0 CA B:ASN124 5.0 9.3 1.0

Manganese binding site 4 out of 4 in the 1.45 A Resolution Crystal Structure of Protein Phosphatase 1


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of 1.45 A Resolution Crystal Structure of Protein Phosphatase 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn402 b:13.6 occ:0.50 O B:HOH508 1.8 13.6 1.0 NE2 B:HIS66 2.1 10.6 1.0 O3 B:PO4403 2.1 20.3 0.8 O B:HOH685 2.2 28.5 1.0 OD2 B:ASP92 2.3 9.3 1.0 OD2 B:ASP64 2.3 13.2 1.0 CE1 B:HIS66 3.0 9.0 1.0 CD2 B:HIS66 3.1 9.8 1.0 MN B:MN401 3.2 9.8 1.0 P B:PO4403 3.3 18.5 0.8 CG B:ASP92 3.4 9.5 1.0 O1 B:PO4403 3.4 11.7 0.8 CG B:ASP64 3.5 9.3 1.0 CB B:ASP92 3.7 8.1 1.0 O2 B:PO4403 3.9 21.7 0.8 O B:HIS248 4.0 20.6 1.0 CB B:ASP64 4.2 9.0 1.0 ND1 B:HIS66 4.2 8.5 1.0 NH1 B:ARG96 4.2 26.3 1.0 CG B:HIS66 4.2 7.8 1.0 CD2 B:HIS125 4.3 9.8 1.0 CE2 B:PHE267 4.3 10.6 1.0 OH B:TYR272 4.4 34.8 1.0 OD1 B:ASP92 4.5 9.4 1.0 OD1 B:ASP64 4.5 10.9 1.0 O4 B:PO4403 4.5 20.1 0.8 NE2 B:HIS125 4.5 10.9 1.0 NE2 B:HIS173 4.5 9.6 1.0 CE1 B:HIS173 4.6 10.2 1.0 CA B:HIS248 4.7 11.0 1.0 C B:HIS248 4.7 13.6 1.0 ND1 B:HIS248 4.8 10.6 1.0 CZ B:PHE267 4.9 12.5 1.0 OD1 B:ASN124 4.9 10.4 1.0

M.S.Choy, M.Hieke, G.S.Kumar, G.R.Lewis, K.R.Gonzalez-Dewhitt, R.P.Kessler, B.J.Stein, M.Hessenberger, A.C.Nairn, W.Peti, R.Page. Understanding the Antagonism of Retinoblastoma Protein Dephosphorylation By Pnuts Provides Insights Into the PP1 Regulatory Code. Proc.Natl.Acad.Sci.Usa V. 111 4097 2014.
ISSN: ISSN 0027-8424
PubMed: 24591642
DOI: 10.1073/PNAS.1317395111