Manganese in PDB 4mp0: Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2

All present enzymatic activity of Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2:
3.1.3.16;

The structure of Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2, PDB code: 4mp0 was solved by M.S.Choy, M.Hieke, W.Peti, R.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.84 / 2.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	92.407, 92.407, 199.342, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 20.2

The binding sites of Manganese atom in the Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2 (pdb code 4mp0). 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 A Second Nuclear PP1 Holoenzyme, Crystal Form 2, PDB code: 4mp0:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:25.2 occ:0.90 O4 A:PO4405 2.1 31.8 1.0 OD2 A:ASP64 2.1 25.9 1.0 O A:HOH642 2.2 28.9 1.0 OD2 A:ASP92 2.2 22.9 1.0 NE2 A:HIS66 2.2 24.7 1.0 O A:HOH538 2.2 30.4 1.0 CE1 A:HIS66 3.1 28.2 1.0 CD2 A:HIS66 3.2 26.8 1.0 CG A:ASP92 3.2 22.3 1.0 MN A:MN402 3.3 22.4 1.0 CG A:ASP64 3.3 25.2 1.0 P A:PO4405 3.3 32.4 0.8 CB A:ASP92 3.6 19.9 1.0 O3 A:PO4405 3.7 31.1 1.0 O A:HOH520 3.7 36.0 1.0 O2 A:PO4405 3.9 28.6 0.9 CB A:ASP64 4.1 23.1 1.0 NH1 A:ARG96 4.1 27.8 1.0 ND1 A:HIS66 4.3 22.2 1.0 OD1 A:ASP64 4.3 25.9 1.0 OD1 A:ASP92 4.3 24.6 1.0 CG A:HIS66 4.3 25.0 1.0 CD2 A:HIS125 4.3 23.1 1.0 OH A:TYR272 4.4 34.8 1.0 CE1 A:HIS173 4.5 23.9 1.0 NE2 A:HIS173 4.5 18.9 1.0 O1 A:PO4405 4.5 33.1 1.0 O A:HIS248 4.5 30.9 1.0 NE2 A:HIS125 4.6 25.1 1.0 CE1 A:PHE267 4.6 26.6 1.0 CA A:HIS248 4.8 25.3 1.0 C A:HIS248 4.9 31.8 1.0 ND1 A:HIS248 4.9 23.6 1.0

Manganese binding site 2 out of 4 in the Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:22.4 occ:0.98 NE2 A:HIS173 2.2 18.9 1.0 OD1 A:ASN124 2.2 23.2 1.0 O A:HOH642 2.2 28.9 1.0 OD2 A:ASP92 2.2 22.9 1.0 O3 A:PO4405 2.2 31.1 1.0 ND1 A:HIS248 2.2 23.6 1.0 CE1 A:HIS248 2.9 27.2 1.0 CE1 A:HIS173 3.1 23.9 1.0 CG A:ASP92 3.1 22.3 1.0 CG A:ASN124 3.1 21.5 1.0 CD2 A:HIS173 3.2 18.2 1.0 MN A:MN401 3.3 25.2 0.9 P A:PO4405 3.3 32.4 0.8 OD1 A:ASP92 3.4 24.6 1.0 CG A:HIS248 3.4 26.3 1.0 O4 A:PO4405 3.4 31.8 1.0 ND2 A:ASN124 3.5 19.4 1.0 CA A:HIS248 3.8 25.3 1.0 O2 A:PO4405 3.9 28.6 0.9 CB A:HIS248 4.0 18.8 1.0 OD2 A:ASP64 4.1 25.9 1.0 NE2 A:HIS248 4.1 26.3 1.0 O A:HIS248 4.1 30.9 1.0 CD2 A:HIS125 4.2 23.1 1.0 ND1 A:HIS173 4.2 18.3 1.0 CG A:HIS173 4.3 20.7 1.0 CD2 A:HIS248 4.4 23.3 1.0 CB A:ASP92 4.4 19.9 1.0 C A:HIS248 4.5 31.8 1.0 CB A:ASN124 4.5 23.2 1.0 O1 A:PO4405 4.6 33.1 1.0 N A:ASN124 4.6 22.3 1.0 O A:LEU205 4.7 23.5 1.0 NE2 A:HIS125 4.8 25.1 1.0 N A:HIS248 4.9 22.9 1.0

Manganese binding site 3 out of 4 in the Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn401 b:39.2 occ:0.96 O2 C:PO4403 2.1 44.6 0.9 OD2 C:ASP64 2.2 49.3 1.0 OD2 C:ASP92 2.2 36.6 1.0 O C:HOH566 2.2 36.5 1.0 O C:HOH567 2.2 41.0 1.0 NE2 C:HIS66 2.2 34.4 1.0 CG C:ASP92 3.1 36.8 1.0 CD2 C:HIS66 3.1 40.5 1.0 CE1 C:HIS66 3.2 34.5 1.0 MN C:MN402 3.3 32.2 0.9 CG C:ASP64 3.3 42.1 1.0 P C:PO4403 3.4 37.8 0.8 CB C:ASP92 3.5 35.2 1.0 O1 C:PO4403 3.7 34.1 1.0 CB C:ASP64 4.0 44.5 1.0 O4 C:PO4403 4.0 39.8 0.9 NH1 C:ARG96 4.1 42.4 1.0 OD1 C:ASP92 4.3 35.9 1.0 OD1 C:ASP64 4.3 48.3 1.0 ND1 C:HIS66 4.3 31.8 1.0 CG C:HIS66 4.3 36.9 1.0 CD2 C:HIS125 4.4 29.2 1.0 OH C:TYR272 4.4 50.6 1.0 CE1 C:HIS173 4.5 44.8 1.0 NE2 C:HIS173 4.5 40.6 1.0 O3 C:PO4403 4.5 43.0 1.0 CE1 C:PHE267 4.5 47.4 1.0 NE2 C:HIS125 4.6 30.8 1.0 O C:HIS248 4.7 46.2 1.0 CA C:HIS248 4.8 44.4 1.0 OD1 C:ASN124 4.9 36.5 1.0 C C:HIS248 4.9 46.4 1.0 CA C:ASP92 5.0 37.3 1.0

Manganese binding site 4 out of 4 in the Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of A Second Nuclear PP1 Holoenzyme, Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn402 b:32.2 occ:0.93 OD1 C:ASN124 2.2 36.5 1.0 O C:HOH566 2.2 36.5 1.0 NE2 C:HIS173 2.2 40.6 1.0 OD2 C:ASP92 2.2 36.6 1.0 O1 C:PO4403 2.2 34.1 1.0 ND1 C:HIS248 2.3 33.8 1.0 CE1 C:HIS248 3.0 36.9 1.0 CE1 C:HIS173 3.1 44.8 1.0 CG C:ASP92 3.1 36.8 1.0 CG C:ASN124 3.1 34.5 1.0 CD2 C:HIS173 3.2 40.5 1.0 MN C:MN401 3.3 39.2 1.0 P C:PO4403 3.3 37.8 0.8 O2 C:PO4403 3.5 44.6 0.9 CG C:HIS248 3.5 42.0 1.0 ND2 C:ASN124 3.5 29.2 1.0 OD1 C:ASP92 3.5 35.9 1.0 CA C:HIS248 3.7 44.4 1.0 O4 C:PO4403 4.0 39.8 0.9 CB C:HIS248 4.0 48.8 1.0 OD2 C:ASP64 4.0 49.3 1.0 O C:HIS248 4.1 46.2 1.0 NE2 C:HIS248 4.2 40.0 1.0 ND1 C:HIS173 4.3 37.5 1.0 CD2 C:HIS125 4.3 29.2 1.0 CG C:HIS173 4.3 43.8 1.0 C C:HIS248 4.4 46.4 1.0 CB C:ASP92 4.4 35.2 1.0 CD2 C:HIS248 4.5 41.0 1.0 CB C:ASN124 4.5 36.0 1.0 O3 C:PO4403 4.6 43.0 1.0 N C:ASN124 4.6 34.8 1.0 O C:LEU205 4.7 37.9 1.0 N C:HIS248 4.7 45.8 1.0 CG C:ASP64 5.0 42.1 1.0 NE2 C:HIS125 5.0 30.8 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