Manganese in PDB 4zx2: Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid

All present enzymatic activity of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid:
3.1.3.16;

The structure of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid, PDB code: 4zx2 was solved by D.Chattopadhyay, M.R.Swingle, E.A.Salter, A.Wierzbicki, R.E.Honkanen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.96 / 1.23
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.600, 90.831, 94.827, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 17.5

The binding sites of Manganese atom in the Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid (pdb code 4zx2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid, PDB code: 4zx2:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:5.7 occ:1.00 O09 A:4TE503 2.1 6.8 1.0 OD1 A:ASN303 2.1 5.8 1.0 NE2 A:HIS352 2.2 4.3 1.0 ND1 A:HIS427 2.2 4.8 1.0 OD2 A:ASP271 2.3 4.4 1.0 C07 A:4TE503 2.9 6.8 1.0 O08 A:4TE503 2.9 6.8 1.0 CD2 A:HIS352 3.1 4.3 1.0 CE1 A:HIS427 3.1 4.9 1.0 CE1 A:HIS352 3.1 4.2 1.0 CG A:ASN303 3.2 5.7 1.0 CG A:ASP271 3.2 4.3 1.0 CG A:HIS427 3.3 4.8 1.0 MN A:MN502 3.4 5.0 1.0 OD1 A:ASP271 3.5 4.5 1.0 CA A:HIS427 3.7 5.0 1.0 ND2 A:ASN303 3.7 6.2 1.0 CB A:HIS427 3.7 4.9 1.0 O14 A:4TE503 3.9 6.9 1.0 OD2 A:ASP242 4.0 4.8 1.0 O A:HIS427 4.2 5.5 1.0 ND1 A:HIS352 4.3 4.2 1.0 CG A:HIS352 4.3 4.2 1.0 NE2 A:HIS427 4.3 4.9 1.0 C06 A:4TE503 4.3 6.9 1.0 CB A:ASN303 4.4 5.5 1.0 CD2 A:HIS427 4.4 4.9 1.0 N A:ASN303 4.4 4.8 1.0 CB A:ASP271 4.5 4.3 1.0 C A:HIS427 4.5 5.3 1.0 CD2 A:HIS304 4.5 5.5 1.0 N A:HIS427 4.7 4.8 1.0 O A:LEU385 4.7 5.3 1.0 C12 A:4TE503 4.7 7.0 1.0 C05 A:4TE503 4.8 7.1 1.0 CG A:ASP242 4.9 4.7 1.0 CA A:ASN303 4.9 5.2 1.0 O10 A:4TE503 5.0 6.8 1.0

Manganese binding site 2 out of 2 in the Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Co-Crystal Structures of PP5 in Complex with 5-Methyl-7- Oxabicyclo[2.2.1]Heptane-2,3-Dicarboxylic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:5.0 occ:1.00 OD2 A:ASP242 2.1 4.8 1.0 NE2 A:HIS244 2.2 5.2 1.0 O09 A:4TE503 2.2 6.8 1.0 O14 A:4TE503 2.2 6.9 1.0 OD2 A:ASP271 2.2 4.4 1.0 O10 A:4TE503 2.3 6.8 1.0 C07 A:4TE503 2.9 6.8 1.0 C05 A:4TE503 3.0 7.1 1.0 CE1 A:HIS244 3.1 5.4 1.0 C12 A:4TE503 3.1 7.0 1.0 CD2 A:HIS244 3.2 5.2 1.0 CG A:ASP271 3.2 4.3 1.0 C02 A:4TE503 3.3 7.1 1.0 CG A:ASP242 3.3 4.7 1.0 C06 A:4TE503 3.3 6.9 1.0 MN A:MN501 3.4 5.7 1.0 C01 A:4TE503 3.4 7.0 1.0 CB A:ASP271 3.6 4.3 1.0 O08 A:4TE503 3.9 6.8 1.0 CB A:ASP242 4.0 4.8 1.0 CD2 A:HIS304 4.2 5.5 1.0 OD1 A:ASP242 4.2 4.8 1.0 ND1 A:HIS244 4.3 5.4 1.0 O13 A:4TE503 4.3 7.4 1.0 OD1 A:ASP271 4.3 4.5 1.0 CG A:HIS244 4.3 5.3 1.0 C04 A:4TE503 4.4 7.5 1.0 C03 A:4TE503 4.5 7.5 1.0 CE1 A:HIS352 4.5 4.2 1.0 NE2 A:HIS352 4.5 4.3 1.0 CE1 A:PHE446 4.6 5.8 1.0 NE2 A:HIS304 4.7 5.6 1.0 CA A:HIS427 4.7 5.0 1.0 OD1 A:ASN303 4.8 5.8 1.0 O A:HIS427 4.9 5.5 1.0 C A:HIS427 5.0 5.3 1.0

D.Chattopadhyay, M.R.Swingle, E.A.Salter, E.Wood, B.D'arcy, C.Zivanov, K.Abney, A.Musiyenko, S.F.Rusin, A.Kettenbach, L.Yet, C.E.Schroeder, J.E.Golden, W.H.Dunham, A.C.Gingras, S.Banerjee, D.Forbes, A.Wierzbicki, R.E.Honkanen. Crystal Structures and Mutagenesis of Ppp-Family Ser/Thr Protein Phosphatases Elucidate the Selectivity of Cantharidin and Novel Norcantharidin-Based Inhibitors of PP5C. Biochem. Pharmacol. V. 109 14 2016.
ISSN: ISSN 1873-2968
PubMed: 27002182
DOI: 10.1016/J.BCP.2016.03.011