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Manganese in PDB 6nts: Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap)

Enzymatic activity of Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap)

All present enzymatic activity of Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap):
3.1.3.16;

Other elements in 6nts:

The structure of Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap) also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap) (pdb code 6nts). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap), PDB code: 6nts:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 6nts

Go back to Manganese Binding Sites List in 6nts
Manganese binding site 1 out of 2 in the Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn401

b:0.1
occ:1.00
ND1 C:HIS241 1.9 0.5 1.0
OD1 C:ASN117 2.4 0.7 1.0
NE2 C:HIS167 2.4 0.1 1.0
OD2 C:ASP85 2.7 0.8 1.0
CE1 C:HIS241 2.7 0.5 1.0
CG C:HIS241 3.1 0.5 1.0
CE1 C:HIS167 3.2 0.1 1.0
MN C:MN402 3.2 0.3 1.0
CD2 C:HIS118 3.3 1.0 1.0
CG C:ASN117 3.4 0.7 1.0
CD2 C:HIS167 3.5 0.1 1.0
CG C:ASP85 3.5 0.8 1.0
NE2 C:HIS118 3.5 1.0 1.0
CA C:HIS241 3.6 0.5 1.0
CB C:HIS241 3.6 0.5 1.0
OD1 C:ASP85 3.7 0.8 1.0
ND2 C:ASN117 3.8 0.7 1.0
NE2 C:HIS241 3.9 0.5 1.0
CD2 C:HIS241 4.1 0.5 1.0
O C:HIS241 4.2 0.5 1.0
ND1 C:HIS167 4.4 0.1 1.0
C C:HIS241 4.4 0.5 1.0
OD2 C:ASP57 4.4 0.4 1.0
CG C:HIS167 4.5 0.1 1.0
CG C:HIS118 4.5 1.0 1.0
N C:HIS241 4.6 0.5 1.0
CB C:ASN117 4.7 0.7 1.0
CE1 C:HIS118 4.8 1.0 1.0
N C:ASN117 4.8 0.7 1.0
CB C:ASP85 4.9 0.8 1.0
O C:LEU199 4.9 0.5 1.0
OD1 C:ASP57 4.9 0.4 1.0
CG C:ASP57 5.0 0.4 1.0
N C:HIS118 5.0 1.0 1.0

Manganese binding site 2 out of 2 in 6nts

Go back to Manganese Binding Sites List in 6nts
Manganese binding site 2 out of 2 in the Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Protein Phosphatase 2A (Aalpha-B56ALPHA-Calpha) Holoenzyme in Complex with A Small Molecule Activator of PP2A (Smap) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn402

b:0.3
occ:1.00
OD2 C:ASP85 2.2 0.8 1.0
NE2 C:HIS59 2.2 0.8 1.0
OD2 C:ASP57 2.8 0.4 1.0
CE1 C:HIS59 3.0 0.8 1.0
MN C:MN401 3.2 0.1 1.0
CG C:ASP85 3.4 0.8 1.0
CD2 C:HIS59 3.4 0.8 1.0
CG C:ASP57 3.4 0.4 1.0
NE2 C:HIS118 3.5 1.0 1.0
O C:HIS241 3.8 0.5 1.0
CD2 C:HIS118 3.9 1.0 1.0
CB C:ASP57 3.9 0.4 1.0
CB C:ASP85 4.0 0.8 1.0
CE1 C:HIS118 4.0 1.0 1.0
OH C:TYR265 4.1 0.8 1.0
OD1 C:ASP57 4.1 0.4 1.0
ND1 C:HIS59 4.2 0.8 1.0
CA C:HIS241 4.4 0.5 1.0
OD1 C:ASP85 4.4 0.8 1.0
CG C:HIS59 4.4 0.8 1.0
ND1 C:HIS241 4.5 0.5 1.0
CG C:HIS118 4.5 1.0 1.0
C C:HIS241 4.6 0.5 1.0
ND1 C:HIS118 4.6 1.0 1.0
CE1 C:HIS167 4.7 0.1 1.0
CE1 C:PHE260 4.7 0.3 1.0
NE2 C:HIS167 4.8 0.1 1.0
CZ C:TYR265 4.9 0.8 1.0

Reference:

D.Leonard, W.Huang, S.Izadmehr, C.M.O'connor, D.D.Wiredja, Z.Wang, N.Zaware, Y.Chen, D.M.Schlatzer, J.Kiselar, N.Vasireddi, S.Schuchner, A.L.Perl, M.D.Galsky, W.Xu, D.L.Brautigan, E.Ogris, D.J.Taylor, G.Narla. Selective PP2A Enhancement Through Biased Heterotrimer Stabilization. Cell 2020.
ISSN: ISSN 1097-4172
PubMed: 32315618
DOI: 10.1016/J.CELL.2020.03.038
Page generated: Tue Dec 15 04:58:00 2020

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