Manganese in PDB 8u89: The Structure of the PP2A-B56DELTA Holoenzyme Mutant - E197K

All present enzymatic activity of The Structure of the PP2A-B56DELTA Holoenzyme Mutant - E197K:
3.1.3.16;

The binding sites of Manganese atom in the The Structure of the PP2A-B56DELTA Holoenzyme Mutant - E197K (pdb code 8u89). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The Structure of the PP2A-B56DELTA Holoenzyme Mutant - E197K, PDB code: 8u89:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the The Structure of the PP2A-B56DELTA Holoenzyme Mutant - E197K


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Structure of the PP2A-B56DELTA Holoenzyme Mutant - E197K within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn401 b:140.9 occ:1.00 OD2 C:ASP85 2.1 97.5 1.0 ND1 C:HIS241 2.2 83.8 1.0 NE2 C:HIS167 2.2 76.0 1.0 OD1 C:ASN117 2.2 63.2 1.0 CE1 C:HIS167 2.6 76.8 1.0 CG C:HIS241 2.7 76.5 1.0 CG C:ASP85 2.8 90.3 1.0 CB C:HIS241 2.9 75.4 1.0 OD1 C:ASP85 3.0 88.0 1.0 MN C:MN402 3.1 123.0 1.0 CE1 C:HIS241 3.2 79.3 1.0 CA C:HIS241 3.2 74.7 1.0 CG C:ASN117 3.3 65.0 1.0 CD2 C:HIS167 3.4 70.2 1.0 OD2 C:ASP57 3.6 81.4 1.0 CD2 C:HIS241 3.8 76.2 1.0 ND1 C:HIS167 3.9 74.6 1.0 ND2 C:ASN117 3.9 71.7 1.0 NE2 C:HIS241 4.0 78.6 1.0 CD2 C:HIS118 4.0 67.7 1.0 CB C:ASP85 4.0 86.3 1.0 N C:HIS241 4.2 78.4 1.0 CG C:HIS167 4.3 67.8 1.0 C C:HIS241 4.3 78.1 1.0 O C:HIS241 4.3 87.4 1.0 CG C:ASP57 4.4 81.5 1.0 N C:ASN117 4.5 77.5 1.0 OD1 C:ASP57 4.5 78.1 1.0 CB C:ASN117 4.6 72.1 1.0 NE2 C:HIS118 4.6 65.9 1.0

Manganese binding site 2 out of 2 in the The Structure of the PP2A-B56DELTA Holoenzyme Mutant - E197K


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The Structure of the PP2A-B56DELTA Holoenzyme Mutant - E197K within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn402 b:123.0 occ:1.00 OD2 C:ASP85 2.1 97.5 1.0 CE1 C:HIS59 2.4 68.0 1.0 OD2 C:ASP57 2.5 81.4 1.0 MN C:MN401 3.1 140.9 1.0 NE2 C:HIS59 3.3 62.1 1.0 CG C:ASP85 3.3 90.3 1.0 ND1 C:HIS59 3.5 62.2 1.0 CG C:ASP57 3.6 81.5 1.0 ND1 C:HIS241 3.6 83.8 1.0 OH C:TYR265 3.9 88.4 1.0 CB C:ASP85 4.0 86.3 1.0 CA C:HIS241 4.1 74.7 1.0 CB C:ASP57 4.1 76.7 1.0 NE2 C:HIS118 4.2 65.9 1.0 CD2 C:HIS118 4.2 67.7 1.0 O C:HIS241 4.3 87.4 1.0 OD1 C:ASP85 4.3 88.0 1.0 CE1 C:PHE260 4.3 80.8 1.0 CE1 C:HIS241 4.4 79.3 1.0 C C:HIS241 4.5 78.1 1.0 CD2 C:HIS59 4.5 60.0 1.0 OD1 C:ASP57 4.5 78.1 1.0 CG C:HIS59 4.6 61.7 1.0 CG C:HIS241 4.7 76.5 1.0 OD1 C:ASN117 4.8 63.2 1.0 CZ C:PHE260 4.8 79.5 1.0 CB C:HIS241 4.9 75.4 1.0 CZ C:TYR265 4.9 80.9 1.0 N C:HIS241 5.0 78.4 1.0

C.G.Wu, V.K.Balakrishnan, R.A.Merrill, P.S.Parihar, K.Konovolov, Y.C.Chen, Z.Xu, H.Wei, R.Sundaresan, Q.Cui, B.E.Wadzinski, M.R.Swingle, A.Musiyenko, W.K.Chung, R.E.Honkanen, A.Suzuki, X.Huang, S.Strack, Y.Xing. B56 Delta Long-Disordered Arms Form A Dynamic PP2A Regulation Interface Coupled with Global Allostery and Jordan'S Syndrome Mutations. Proc.Natl.Acad.Sci.Usa V. 121 27120 2024.
ISSN: ESSN 1091-6490
PubMed: 38150499
DOI: 10.1073/PNAS.2310727120