Manganese in PDB 1u32: Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid

All present enzymatic activity of Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid:
3.1.3.16;

The structure of Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid, PDB code: 1u32 was solved by J.T.Maynes, K.R.Perreault, M.M.Cherney, H.A.Luu, M.N.G.James, C.F.B.Holmes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.01 / 2.00
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	98.759, 98.759, 62.180, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 25.4

The binding sites of Manganese atom in the Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid (pdb code 1u32). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid, PDB code: 1u32:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn400 b:18.6 occ:1.00 OD1 A:ASN124 2.2 14.9 1.0 OD2 A:ASP92 2.2 10.9 1.0 NE2 A:HIS173 2.3 15.7 1.0 ND1 A:HIS248 2.3 15.0 1.0 O A:HOH505 3.0 34.6 1.0 CE1 A:HIS248 3.0 13.7 1.0 CG A:ASP92 3.1 16.9 1.0 CD2 A:HIS173 3.2 14.9 1.0 CG A:ASN124 3.2 15.4 1.0 CE1 A:HIS173 3.3 15.1 1.0 MN A:MN401 3.3 22.3 1.0 OD1 A:ASP92 3.4 13.0 1.0 CG A:HIS248 3.4 15.7 1.0 CA A:HIS248 3.7 16.5 1.0 ND2 A:ASN124 3.7 12.8 1.0 CB A:HIS248 3.9 14.8 1.0 O A:HIS248 4.0 18.4 1.0 CD2 A:HIS125 4.1 15.8 1.0 OD2 A:ASP64 4.1 12.5 1.0 NE2 A:HIS248 4.2 15.4 1.0 C A:HIS248 4.3 17.4 1.0 CG A:HIS173 4.4 14.2 1.0 ND1 A:HIS173 4.4 15.1 1.0 CB A:ASP92 4.4 13.7 1.0 CD2 A:HIS248 4.4 13.2 1.0 N A:ASN124 4.5 13.8 1.0 CB A:ASN124 4.5 15.0 1.0 N A:HIS248 4.6 14.0 1.0 NE2 A:HIS125 4.7 13.3 1.0 O A:LEU205 4.8 17.9 1.0 CG A:ASP64 4.9 17.4 1.0 OD1 A:ASP64 5.0 14.0 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of A Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:22.3 occ:1.00 OD2 A:ASP64 2.1 12.5 1.0 OD2 A:ASP92 2.2 10.9 1.0 NE2 A:HIS66 2.3 14.4 1.0 CE1 A:HIS66 3.2 18.2 1.0 CG A:ASP64 3.2 17.4 1.0 CG A:ASP92 3.2 16.9 1.0 CD2 A:HIS66 3.3 15.4 1.0 MN A:MN400 3.3 18.6 1.0 O A:HOH505 3.4 34.6 1.0 CB A:ASP92 3.7 13.7 1.0 CB A:ASP64 4.0 17.0 1.0 OD1 A:ASP64 4.1 14.0 1.0 CD2 A:HIS125 4.1 15.8 1.0 O A:HIS248 4.2 18.4 1.0 O A:HOH566 4.3 41.9 1.0 OD1 A:ASP92 4.3 13.0 1.0 ND1 A:HIS66 4.3 15.8 1.0 CG A:HIS66 4.4 15.1 1.0 CE1 A:PHE267 4.4 17.8 1.0 NE2 A:HIS125 4.4 13.3 1.0 NE2 A:HIS173 4.5 15.7 1.0 OH A:TYR272 4.6 24.1 1.0 CA A:HIS248 4.6 16.5 1.0 C A:HIS248 4.6 17.4 1.0 CE1 A:HIS173 4.7 15.1 1.0 ND1 A:HIS248 5.0 15.0 1.0

J.T.Maynes, K.R.Perreault, M.M.Cherney, H.A.Luu, M.N.G.James, C.F.B.Holmes. Crystal Structure and Mutagenesis of A Protein Phosphatase-1:Calcineurin Hybrid Elucidate the Role of the {Beta}12-{Beta}13 Loop in Inhibitor Binding J.Biol.Chem. V. 279 43198 2004.
ISSN: ISSN 0021-9258
PubMed: 15280359
DOI: 10.1074/JBC.M407184200