Manganese in PDB 4ut2: X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate

All present enzymatic activity of X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate:
3.1.3.16;

The structure of X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate, PDB code: 4ut2 was solved by J.Kopec, M.Zeh Silva, C.Fotinou, R.A.Steiner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	64.12 / 1.96
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.550, 90.240, 91.130, 90.00, 90.05, 90.00
R / Rfree (%)	16.667 / 20.065

The binding sites of Manganese atom in the X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate (pdb code 4ut2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate, PDB code: 4ut2:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn400 b:25.5 occ:1.00 O A:HOH2040 2.0 26.7 1.0 OD2 A:ASP64 2.1 22.3 1.0 NE2 A:HIS66 2.2 22.0 1.0 OD2 A:ASP92 2.3 20.7 1.0 O2 A:PO4501 2.4 35.4 1.0 O A:HOH2041 2.4 21.2 1.0 CD2 A:HIS66 3.2 21.6 1.0 CE1 A:HIS66 3.2 21.6 1.0 CG A:ASP64 3.3 20.9 1.0 CG A:ASP92 3.3 20.1 1.0 MN A:MN401 3.3 20.0 1.0 P A:PO4501 3.4 36.4 1.0 O3 A:PO4501 3.6 35.0 1.0 CB A:ASP92 3.6 19.2 1.0 O4 A:PO4501 4.0 35.1 1.0 CB A:ASP64 4.0 20.9 1.0 OD1 A:ASP64 4.2 21.9 1.0 O A:HOH2116 4.2 23.4 1.0 CD2 A:HIS125 4.3 24.1 1.0 ND1 A:HIS66 4.3 22.0 1.0 CG A:HIS66 4.3 21.9 1.0 NH1 A:ARG96 4.4 44.4 1.0 OD1 A:ASP92 4.4 21.8 1.0 OH A:TYR272 4.4 31.2 1.0 NE2 A:HIS173 4.4 21.9 1.0 NE2 A:HIS125 4.4 24.5 1.0 CE1 A:HIS173 4.5 21.5 1.0 O A:HIS248 4.6 22.0 1.0 CE1 A:PHE267 4.7 22.3 1.0 CA A:HIS248 4.7 22.1 1.0 O1 A:PO4501 4.7 38.6 1.0 C A:HIS248 4.8 22.9 1.0 ND1 A:HIS248 5.0 20.9 1.0

Manganese binding site 2 out of 4 in the X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:20.0 occ:1.00 O3 A:PO4501 2.0 35.0 1.0 O A:HOH2040 2.1 26.7 1.0 OD1 A:ASN124 2.2 20.9 1.0 ND1 A:HIS248 2.2 20.9 1.0 OD2 A:ASP92 2.3 20.7 1.0 NE2 A:HIS173 2.4 21.9 1.0 CE1 A:HIS248 2.9 20.6 1.0 CG A:ASN124 3.2 21.9 1.0 CD2 A:HIS173 3.2 21.5 1.0 P A:PO4501 3.3 36.4 1.0 MN A:MN400 3.3 25.5 1.0 CG A:ASP92 3.3 20.1 1.0 CG A:HIS248 3.4 20.8 1.0 CE1 A:HIS173 3.4 21.5 1.0 ND2 A:ASN124 3.6 22.6 1.0 O2 A:PO4501 3.6 35.4 1.0 CA A:HIS248 3.7 22.1 1.0 OD1 A:ASP92 3.7 21.8 1.0 O4 A:PO4501 3.8 35.1 1.0 CB A:HIS248 3.9 21.8 1.0 O A:HIS248 4.0 22.0 1.0 NE2 A:HIS248 4.1 20.7 1.0 OD2 A:ASP64 4.2 22.3 1.0 CD2 A:HIS125 4.2 24.1 1.0 CD2 A:HIS248 4.4 21.4 1.0 C A:HIS248 4.4 22.9 1.0 CG A:HIS173 4.4 22.1 1.0 O1 A:PO4501 4.5 38.6 1.0 ND1 A:HIS173 4.5 22.4 1.0 CB A:ASN124 4.5 22.6 1.0 CB A:ASP92 4.6 19.2 1.0 N A:ASN124 4.6 22.0 1.0 O A:LEU205 4.7 22.7 1.0 NE2 A:HIS125 4.7 24.5 1.0 N A:HIS248 4.8 22.0 1.0

Manganese binding site 3 out of 4 in the X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn400 b:21.5 occ:1.00 O B:HOH2038 2.0 23.9 1.0 O B:HOH2039 2.1 25.8 1.0 OD2 B:ASP64 2.1 22.8 1.0 O4 B:PO4501 2.4 36.3 1.0 NE2 B:HIS66 2.4 20.5 1.0 OD2 B:ASP92 2.5 18.5 1.0 CD2 B:HIS66 3.3 20.4 1.0 CG B:ASP64 3.3 22.3 1.0 MN B:MN401 3.4 20.8 1.0 CE1 B:HIS66 3.4 20.0 1.0 P B:PO4501 3.4 37.3 1.0 CG B:ASP92 3.5 18.4 1.0 O1 B:PO4501 3.7 34.6 1.0 O B:HOH2090 3.7 39.8 1.0 CB B:ASP92 3.8 18.3 1.0 O2 B:PO4501 3.9 37.1 1.0 CB B:ASP64 4.0 21.9 1.0 OD1 B:ASP64 4.2 24.0 1.0 OH B:TYR272 4.3 28.9 1.0 CD2 B:HIS125 4.4 18.5 1.0 NH1 B:ARG96 4.4 34.1 1.0 O B:HIS248 4.4 26.9 1.0 CG B:HIS66 4.4 19.8 1.0 ND1 B:HIS66 4.5 19.8 1.0 NE2 B:HIS173 4.5 20.6 1.0 NE2 B:HIS125 4.5 18.6 1.0 OD1 B:ASP92 4.6 18.1 1.0 CE1 B:PHE267 4.6 22.2 1.0 CA B:HIS248 4.6 25.5 1.0 CE1 B:HIS173 4.6 20.0 1.0 C B:HIS248 4.7 26.1 1.0 O3 B:PO4501 4.7 38.5 1.0 ND1 B:HIS248 4.9 25.3 1.0

Manganese binding site 4 out of 4 in the X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of X-Ray Structure of the Human PP1 Gamma Catalytic Subunit Treated with Ascorbate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:20.8 occ:1.00 O B:HOH2038 2.0 23.9 1.0 OD1 B:ASN124 2.1 18.4 1.0 NE2 B:HIS173 2.2 20.6 1.0 OD2 B:ASP92 2.2 18.5 1.0 ND1 B:HIS248 2.2 25.3 1.0 O1 B:PO4501 2.5 34.6 1.0 CE1 B:HIS248 3.0 24.9 1.0 CD2 B:HIS173 3.1 20.4 1.0 CG B:ASN124 3.2 18.7 1.0 CG B:ASP92 3.2 18.4 1.0 CE1 B:HIS173 3.2 20.0 1.0 MN B:MN400 3.4 21.5 1.0 CG B:HIS248 3.4 25.0 1.0 P B:PO4501 3.6 37.3 1.0 OD1 B:ASP92 3.6 18.1 1.0 ND2 B:ASN124 3.7 18.7 1.0 CA B:HIS248 3.7 25.5 1.0 O4 B:PO4501 3.8 36.3 1.0 CB B:HIS248 3.9 25.2 1.0 O2 B:PO4501 4.0 37.1 1.0 OD2 B:ASP64 4.1 22.8 1.0 O B:HIS248 4.2 26.9 1.0 NE2 B:HIS248 4.2 24.9 1.0 CD2 B:HIS125 4.2 18.5 1.0 CG B:HIS173 4.3 21.2 1.0 ND1 B:HIS173 4.3 20.4 1.0 CD2 B:HIS248 4.4 25.0 1.0 C B:HIS248 4.4 26.1 1.0 CB B:ASP92 4.5 18.3 1.0 CB B:ASN124 4.5 18.9 1.0 N B:ASN124 4.5 19.2 1.0 O B:LEU205 4.6 25.5 1.0 N B:HIS248 4.8 24.7 1.0 NE2 B:HIS125 4.8 18.6 1.0 O3 B:PO4501 4.9 38.5 1.0 CG B:ASP64 5.0 22.3 1.0

C.X.Santos, A.D.Hafstad, M.Beretta, M.Zhang, C.Molenaar, J.Kopec, D.Fotinou, T.V.Murray, A.M.Cobb, D.Martin, M.Zeh Silva, N.Anilkumar, K.Schroder, C.M.Shanahan, A.C.Brewer, R.P.Brandes, E.Blanc, M.Parsons, V.Belousov, R.Cammack, R.C.Hider, R.A.Steiner, A.M.Shah. Targeted Redox Inhibition of Protein Phosphatase 1 By NOX4 Regulates EIF2ALPHA-Mediated Stress Signaling. Embo J. V. 35 319 2016.
ISSN: ISSN 0261-4189
PubMed: 26742780
DOI: 10.15252/EMBJ.201592394