Manganese in PDB 1s95: Structure of Serine/Threonine Protein Phosphatase 5

All present enzymatic activity of Structure of Serine/Threonine Protein Phosphatase 5:
3.1.3.16;

The structure of Structure of Serine/Threonine Protein Phosphatase 5, PDB code: 1s95 was solved by M.R.Swingle, R.E.Honkanen, E.M.Ciszak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	40.808, 80.309, 92.189, 90.00, 94.25, 90.00
R / Rfree (%)	16.9 / 20.9

The binding sites of Manganese atom in the Structure of Serine/Threonine Protein Phosphatase 5 (pdb code 1s95). 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 Serine/Threonine Protein Phosphatase 5, PDB code: 1s95:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Structure of Serine/Threonine Protein Phosphatase 5


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Serine/Threonine Protein Phosphatase 5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:24.4 occ:1.00 OD2 A:ASP242 2.1 25.9 1.0 O A:HOH3002 2.1 24.0 1.0 NE2 A:HIS244 2.2 28.8 1.0 OD2 A:ASP271 2.2 26.3 1.0 O1 A:PO41001 2.2 27.0 1.0 O A:HOH3003 2.3 22.6 1.0 CE1 A:HIS244 3.1 26.5 1.0 CD2 A:HIS244 3.2 29.9 1.0 CG A:ASP271 3.2 26.8 1.0 MN A:MN502 3.2 21.6 1.0 P A:PO41001 3.3 28.6 1.0 CG A:ASP242 3.3 30.3 1.0 O3 A:PO41001 3.6 29.2 1.0 O2 A:PO41001 3.7 28.0 1.0 CB A:ASP271 3.7 24.9 1.0 O A:HOH3175 4.0 39.3 1.0 CB A:ASP242 4.1 26.1 1.0 OD1 A:ASP242 4.2 28.4 1.0 NH1 A:ARG275 4.2 32.4 1.0 ND1 A:HIS244 4.3 27.2 1.0 CD2 A:HIS304 4.3 27.2 1.0 CG A:HIS244 4.3 27.1 1.0 OD1 A:ASP271 4.3 27.5 1.0 OH A:TYR451 4.4 31.2 1.0 CE1 A:PHE446 4.4 29.7 1.0 O A:HIS427 4.4 28.8 1.0 NE2 A:HIS352 4.5 24.1 1.0 CE1 A:HIS352 4.5 28.7 1.0 CA A:HIS427 4.6 26.9 1.0 O4 A:PO41001 4.7 27.3 1.0 C A:HIS427 4.7 27.6 1.0 NE2 A:HIS304 4.8 26.6 1.0 OD1 A:ASN303 4.9 29.8 1.0 ND1 A:HIS427 5.0 26.3 1.0

Manganese binding site 2 out of 4 in the Structure of Serine/Threonine Protein Phosphatase 5


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Serine/Threonine Protein Phosphatase 5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:21.6 occ:1.00 O A:HOH3002 2.1 24.0 1.0 OD1 A:ASN303 2.1 29.8 1.0 ND1 A:HIS427 2.2 26.3 1.0 NE2 A:HIS352 2.3 24.1 1.0 O2 A:PO41001 2.3 28.0 1.0 OD2 A:ASP271 2.3 26.3 1.0 CG A:ASN303 3.1 29.1 1.0 CE1 A:HIS427 3.1 28.6 1.0 CD2 A:HIS352 3.2 28.8 1.0 CG A:ASP271 3.2 26.8 1.0 MN A:MN501 3.2 24.4 1.0 CE1 A:HIS352 3.2 28.7 1.0 CG A:HIS427 3.3 26.5 1.0 P A:PO41001 3.4 28.6 1.0 ND2 A:ASN303 3.5 28.0 1.0 OD1 A:ASP271 3.6 27.5 1.0 O1 A:PO41001 3.6 27.0 1.0 CA A:HIS427 3.7 26.9 1.0 CB A:HIS427 3.7 26.7 1.0 O3 A:PO41001 3.9 29.2 1.0 OD2 A:ASP242 4.0 25.9 1.0 O A:HIS427 4.1 28.8 1.0 NE2 A:HIS427 4.3 25.0 1.0 CD2 A:HIS304 4.3 27.2 1.0 C A:HIS427 4.3 27.6 1.0 ND1 A:HIS352 4.4 23.3 1.0 CD2 A:HIS427 4.4 24.7 1.0 CG A:HIS352 4.4 26.1 1.0 CB A:ASN303 4.4 26.6 1.0 N A:ASN303 4.4 26.5 1.0 CB A:ASP271 4.5 24.9 1.0 O4 A:PO41001 4.7 27.3 1.0 O A:LEU385 4.7 29.1 1.0 N A:HIS427 4.8 26.4 1.0 NH1 A:ARG400 4.8 32.9 1.0 CA A:ASN303 4.9 25.2 1.0 CG A:ASP242 5.0 30.3 1.0

Manganese binding site 3 out of 4 in the Structure of Serine/Threonine Protein Phosphatase 5


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of Serine/Threonine Protein Phosphatase 5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn601 b:19.0 occ:1.00 O B:HOH3003 2.0 17.9 1.0 OD2 B:ASP242 2.1 25.0 1.0 NE2 B:HIS244 2.2 26.5 1.0 O1 B:PO42001 2.2 20.0 1.0 OD2 B:ASP271 2.2 24.9 1.0 O B:HOH3004 2.4 16.6 1.0 CE1 B:HIS244 3.1 27.6 1.0 CD2 B:HIS244 3.2 27.4 1.0 MN B:MN602 3.2 14.6 1.0 CG B:ASP271 3.3 28.9 1.0 P B:PO42001 3.3 21.1 1.0 CG B:ASP242 3.3 29.6 1.0 CB B:ASP271 3.7 26.3 1.0 O2 B:PO42001 3.7 21.5 1.0 O3 B:PO42001 3.9 21.6 1.0 CB B:ASP242 4.1 24.9 1.0 OD1 B:ASP242 4.2 27.2 1.0 ND1 B:HIS244 4.2 24.6 1.0 CD2 B:HIS304 4.3 27.8 1.0 CG B:HIS244 4.3 23.6 1.0 OD1 B:ASP271 4.3 24.6 1.0 O B:HOH3087 4.3 32.4 1.0 NH1 B:ARG275 4.3 34.9 1.0 CE1 B:HIS352 4.3 25.4 1.0 NE2 B:HIS352 4.4 27.9 1.0 OH B:TYR451 4.4 29.4 1.0 O B:HIS427 4.4 27.5 1.0 CE1 B:PHE446 4.5 26.5 1.0 O4 B:PO42001 4.6 21.2 1.0 CA B:HIS427 4.7 25.8 1.0 NE2 B:HIS304 4.7 24.1 1.0 C B:HIS427 4.8 26.0 1.0 OD1 B:ASN303 4.9 25.1 1.0 ND1 B:HIS427 4.9 24.8 1.0

Manganese binding site 4 out of 4 in the Structure of Serine/Threonine Protein Phosphatase 5


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of Serine/Threonine Protein Phosphatase 5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn602 b:14.6 occ:1.00 NE2 B:HIS352 2.1 27.9 1.0 OD1 B:ASN303 2.2 25.1 1.0 O B:HOH3003 2.2 17.9 1.0 O2 B:PO42001 2.2 21.5 1.0 ND1 B:HIS427 2.3 24.8 1.0 OD2 B:ASP271 2.4 24.9 1.0 CE1 B:HIS427 3.1 24.9 1.0 CE1 B:HIS352 3.1 25.4 1.0 CG B:ASN303 3.1 25.6 1.0 CD2 B:HIS352 3.2 27.4 1.0 MN B:MN601 3.2 19.0 1.0 CG B:ASP271 3.2 28.9 1.0 P B:PO42001 3.3 21.1 1.0 CG B:HIS427 3.4 26.6 1.0 OD1 B:ASP271 3.5 24.6 1.0 ND2 B:ASN303 3.5 25.7 1.0 O1 B:PO42001 3.6 20.0 1.0 CA B:HIS427 3.8 25.8 1.0 CB B:HIS427 3.9 27.0 1.0 OD2 B:ASP242 4.0 25.0 1.0 O3 B:PO42001 4.1 21.6 1.0 O B:HIS427 4.2 27.5 1.0 CD2 B:HIS304 4.2 27.8 1.0 ND1 B:HIS352 4.2 25.6 1.0 NE2 B:HIS427 4.3 23.9 1.0 CG B:HIS352 4.3 25.1 1.0 N B:ASN303 4.4 22.6 1.0 CD2 B:HIS427 4.4 24.7 1.0 CB B:ASP271 4.5 26.3 1.0 CB B:ASN303 4.5 25.2 1.0 C B:HIS427 4.5 26.0 1.0 O4 B:PO42001 4.6 21.2 1.0 O B:LEU385 4.7 25.3 1.0 N B:HIS427 4.8 26.3 1.0 NE2 B:HIS304 4.9 24.1 1.0 CA B:ASN303 5.0 24.2 1.0 NH1 B:ARG400 5.0 31.3 1.0 CG B:ASP242 5.0 29.6 1.0

M.R.Swingle, R.E.Honkanen, E.M.Ciszak. Structural Basis For the Catalytic Activity of Human Serine/Threonine Protein Phosphatase-5. J.Biol.Chem. V. 279 33992 2004.
ISSN: ISSN 0021-9258
PubMed: 15155720
DOI: 10.1074/JBC.M402855200