Manganese in PDB 6zef: Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25

All present enzymatic activity of Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25:
3.1.3.16;

The structure of Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25, PDB code: 6zef was solved by S.Mouilleron, R.Treisman, R.Fedoryshchak, R.Lee, A.M.Butler, M.Prechova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.05 / 1.94
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	47.510, 57.550, 89.614, 78.08, 74.67, 81.66
R / Rfree (%)	18.2 / 21.2

The structure of Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25 (pdb code 6zef). 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(7-300) Bound to PHACTR1 (516-580) at pH 5.25, PDB code: 6zef:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25


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(7-300) Bound to PHACTR1 (516-580) at pH 5.25 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn406 b:64.4 occ:1.00 O A:HOH556 2.1 54.1 1.0 ND1 A:HIS248 2.7 33.7 1.0 HA A:HIS248 2.7 36.3 1.0 OD2 A:ASP92 2.7 29.0 1.0 OD1 A:ASN124 3.1 28.7 1.0 O A:HIS248 3.3 37.9 1.0 HD21 A:ASN124 3.3 35.1 1.0 HE1 A:HIS248 3.4 41.0 1.0 CE1 A:HIS248 3.4 34.1 1.0 NE2 A:HIS173 3.4 27.4 1.0 HD2 A:HIS125 3.5 33.8 1.0 CA A:HIS248 3.6 30.1 1.0 OD2 A:ASP64 3.6 33.5 1.0 C A:HIS248 3.8 30.5 1.0 CG A:HIS248 3.8 31.6 1.0 CG A:ASN124 3.9 28.3 1.0 ND2 A:ASN124 3.9 29.1 1.0 CG A:ASP92 4.0 28.0 1.0 HE1 A:HIS173 4.1 33.3 1.0 MN A:MN407 4.1 93.0 1.0 CE1 A:HIS173 4.2 27.7 1.0 CB A:HIS248 4.2 30.2 1.0 CD2 A:HIS125 4.2 28.1 1.0 NE2 A:HIS125 4.4 29.7 1.0 HH12 A:ARG221 4.5 56.3 1.0 CD2 A:HIS173 4.5 26.0 1.0 HB2 A:HIS248 4.5 36.3 1.0 NE2 A:HIS66 4.5 32.6 1.0 OD1 A:ASP92 4.6 28.0 1.0 H A:HIS248 4.6 34.1 1.0 NE2 A:HIS248 4.6 34.6 1.0 HD2 A:HIS173 4.6 31.3 1.0 N A:HIS248 4.7 28.3 1.0 CG A:ASP64 4.7 30.6 1.0 HD22 A:ASN124 4.7 35.1 1.0 CD2 A:HIS248 4.8 32.2 1.0 HH22 A:ARG221 4.8 50.1 1.0 HE1 A:HIS66 4.8 38.6 1.0 OD1 A:ASP64 4.9 29.7 1.0 NH1 A:ARG221 4.9 46.8 1.0 N A:GLN249 5.0 30.7 1.0 HB3 A:HIS248 5.0 36.3 1.0

Manganese binding site 2 out of 4 in the Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25


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(7-300) Bound to PHACTR1 (516-580) at pH 5.25 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn407 b:93.0 occ:1.00 O A:HOH556 2.5 54.1 1.0 HH A:TYR272 3.0 47.1 1.0 HE2 A:TYR272 3.4 42.7 1.0 HG23 A:VAL250 3.6 41.6 0.5 OH A:TYR272 3.7 39.1 1.0 HE1 A:PHE267 3.9 40.5 1.0 O A:HOH576 3.9 43.6 1.0 CE2 A:TYR272 4.0 35.5 1.0 MN A:MN406 4.1 64.4 1.0 CZ A:TYR272 4.2 38.7 1.0 HG22 A:VAL250 4.2 41.6 0.5 CG2 A:VAL250 4.3 34.6 0.5 NE2 A:HIS66 4.3 32.6 1.0 O A:HIS248 4.4 37.9 1.0 HG21 A:VAL250 4.5 41.6 0.5 HH12 A:ARG221 4.5 56.3 1.0 H A:VAL250 4.6 40.8 0.5 H A:VAL250 4.6 40.8 0.5 CE1 A:PHE267 4.6 33.6 1.0 HZ A:PHE267 4.7 38.8 1.0 HA A:GLN249 4.7 38.5 1.0 HD2 A:HIS66 4.7 39.4 1.0 OD2 A:ASP64 4.8 33.5 1.0 HB A:VAL250 4.8 41.1 0.5 CD2 A:HIS66 4.9 32.8 1.0 HE A:ARG96 4.9 63.7 1.0

Manganese binding site 3 out of 4 in the Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25


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(7-300) Bound to PHACTR1 (516-580) at pH 5.25 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn404 b:65.4 occ:1.00 HE2 B:HIS173 2.1 32.5 1.0 ND1 B:HIS248 2.5 35.6 1.0 HA B:HIS248 2.6 35.8 1.0 O B:HOH591 2.6 65.8 1.0 OD2 B:ASP92 2.6 29.2 1.0 OD1 B:ASN124 2.8 29.5 1.0 NE2 B:HIS173 3.0 27.0 1.0 O B:HOH571 3.0 48.0 1.0 CE1 B:HIS248 3.3 36.5 1.0 HD21 B:ASN124 3.3 38.3 1.0 HE1 B:HIS248 3.3 44.0 1.0 CA B:HIS248 3.5 29.7 1.0 HD2 B:HIS125 3.5 35.4 1.0 O B:HIS248 3.5 39.5 1.0 CG B:HIS248 3.6 33.7 1.0 CG B:ASN124 3.6 29.7 1.0 OD2 B:ASP64 3.7 35.9 1.0 HE1 B:HIS173 3.7 32.9 1.0 CE1 B:HIS173 3.7 27.3 1.0 CG B:ASP92 3.7 27.3 1.0 ND2 B:ASN124 3.8 31.8 1.0 MN B:MN405 3.9 87.4 1.0 C B:HIS248 3.9 33.3 1.0 CB B:HIS248 4.0 30.4 1.0 CD2 B:HIS173 4.0 27.1 1.0 HD2 B:HIS173 4.2 32.6 1.0 HB2 B:HIS248 4.2 36.6 1.0 OD1 B:ASP92 4.3 26.2 1.0 CD2 B:HIS125 4.3 29.4 1.0 H B:HIS248 4.4 34.3 1.0 NE2 B:HIS248 4.5 36.0 1.0 N B:HIS248 4.5 28.5 1.0 HD22 B:ASN124 4.6 38.3 1.0 H B:ASN124 4.6 30.2 1.0 NE2 B:HIS125 4.6 29.7 1.0 CD2 B:HIS248 4.6 32.7 1.0 CG B:ASP64 4.7 29.9 1.0 HH12 B:ARG221 4.8 56.9 1.0 NE2 B:HIS66 4.8 32.5 1.0 OD1 B:ASP64 4.8 30.6 1.0 HB3 B:HIS248 4.9 36.6 1.0 CB B:ASP92 4.9 27.8 1.0 ND1 B:HIS173 4.9 26.2 1.0 HB2 B:ASP92 4.9 33.5 1.0

Manganese binding site 4 out of 4 in the Structure of PP1(7-300) Bound to PHACTR1 (516-580) at pH 5.25


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(7-300) Bound to PHACTR1 (516-580) at pH 5.25 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn405 b:87.4 occ:1.00 O B:HOH591 2.3 65.8 1.0 HH B:TYR272 3.0 48.5 1.0 HE1 B:PHE267 3.4 41.9 1.0 NE2 B:HIS66 3.5 32.5 1.0 OH B:TYR272 3.5 40.3 1.0 O B:HOH571 3.8 48.0 1.0 MN B:MN404 3.9 65.4 1.0 HE2 B:TYR272 3.9 45.1 1.0 OD2 B:ASP64 3.9 35.9 1.0 HD2 B:HIS66 4.1 37.4 1.0 CZ B:TYR272 4.2 40.5 1.0 CD2 B:HIS66 4.2 31.0 1.0 CE1 B:PHE267 4.2 34.8 1.0 HZ B:PHE267 4.3 39.9 1.0 CE2 B:TYR272 4.3 37.5 1.0 O B:HIS248 4.4 39.5 1.0 CE1 B:HIS66 4.4 30.5 1.0 HE1 B:HIS66 4.6 36.7 1.0 OD2 B:ASP92 4.6 29.2 1.0 CZ B:PHE267 4.7 33.1 1.0 NE2 B:HIS125 4.8 29.7 1.0 HA B:GLN249 4.8 37.7 1.0 C B:HIS248 4.9 33.3 1.0 HH12 B:ARG221 4.9 56.9 1.0 HA B:HIS248 4.9 35.8 1.0 HH21 B:ARG96 4.9 68.3 1.0 HE B:ARG96 4.9 60.1 1.0 H B:VAL250 5.0 39.8 1.0

R.O.Fedoryshchak, M.Prechova, A.Butler, R.Lee, N.O'reilly, H.R.Flynn, A.P.Snijders, N.Eder, S.Ultanir, S.Mouilleron, R.Treisman. Molecular Basis For Substrate Specificity of the PHACTR1/PP1 Phosphatase Holoenzyme. Elife V. 9 2020.
ISSN: ESSN 2050-084X
PubMed: 32975518
DOI: 10.7554/ELIFE.61509