Manganese in PDB 7sd0: Cryo-Em Structure of the SHOC2:PP1C:Mras Complex

All present enzymatic activity of Cryo-Em Structure of the SHOC2:PP1C:Mras Complex:
3.1.3.16; 3.6.5.2;

The structure of Cryo-Em Structure of the SHOC2:PP1C:Mras Complex also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Manganese atom in the Cryo-Em Structure of the SHOC2:PP1C:Mras Complex (pdb code 7sd0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Cryo-Em Structure of the SHOC2:PP1C:Mras Complex, PDB code: 7sd0:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Cryo-Em Structure of the SHOC2:PP1C:Mras Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Cryo-Em Structure of the SHOC2:PP1C:Mras Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn400 b:118.4 occ:1.00 OD1 C:ASN124 1.8 127.2 1.0 NE2 C:HIS173 2.3 127.2 1.0 ND1 C:HIS248 2.3 127.2 1.0 OD2 C:ASP92 2.4 127.2 1.0 CG C:ASN124 2.8 127.2 1.0 CG C:ASP92 3.0 127.2 1.0 CE1 C:HIS248 3.1 127.2 1.0 CE1 C:HIS173 3.2 127.2 1.0 CD2 C:HIS173 3.2 127.2 1.0 ND2 C:ASN124 3.3 127.2 1.0 MN C:MN401 3.3 127.3 1.0 CA C:HIS248 3.3 127.2 1.0 O C:HIS248 3.3 127.2 1.0 CG C:HIS248 3.3 127.2 1.0 OD1 C:ASP92 3.4 127.2 1.0 C C:HIS248 3.8 127.2 1.0 CB C:HIS248 3.8 127.2 1.0 CB C:ASN124 4.1 127.2 1.0 CB C:ASP92 4.1 127.2 1.0 CD2 C:HIS125 4.2 127.2 1.0 NE2 C:HIS248 4.2 127.2 1.0 N C:HIS248 4.3 127.2 1.0 N C:ASN124 4.3 127.2 1.0 ND1 C:HIS173 4.3 127.2 1.0 CG C:HIS173 4.4 127.2 1.0 CD2 C:HIS248 4.4 127.2 1.0 NE2 C:HIS125 4.7 127.2 1.0 OD2 C:ASP64 4.7 127.2 1.0 CA C:ASN124 4.8 127.2 1.0

Manganese binding site 2 out of 2 in the Cryo-Em Structure of the SHOC2:PP1C:Mras Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Cryo-Em Structure of the SHOC2:PP1C:Mras Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn401 b:127.3 occ:1.00 O C:HIS248 2.5 127.2 1.0 OD2 C:ASP92 2.5 127.2 1.0 OD2 C:ASP64 2.7 127.2 1.0 NE2 C:HIS66 2.9 127.2 1.0 MN C:MN400 3.3 118.4 1.0 C C:HIS248 3.5 127.2 1.0 CD2 C:HIS66 3.7 127.2 1.0 CG C:ASP92 3.7 127.2 1.0 CG C:ASP64 3.9 127.2 1.0 CE1 C:HIS66 3.9 127.2 1.0 CA C:HIS248 4.0 127.2 1.0 CB C:ASP92 4.2 127.2 1.0 OH C:TYR272 4.4 128.0 1.0 CB C:ASP64 4.4 127.2 1.0 N C:GLN249 4.5 127.2 1.0 O C:GLN249 4.6 127.2 1.0 OD1 C:ASP92 4.7 127.2 1.0 OD1 C:ASN124 4.7 127.2 1.0 NE2 C:HIS125 4.8 127.2 1.0 NE2 C:HIS173 4.8 127.2 1.0 CD2 C:HIS125 4.8 127.2 1.0 N C:HIS248 4.8 127.2 1.0 OD1 C:ASP64 4.8 127.2 1.0 CE1 C:HIS173 4.9 127.2 1.0 CA C:GLN249 4.9 127.2 1.0 CG C:HIS66 4.9 127.2 1.0 CE1 C:PHE267 4.9 127.2 1.0 C C:GLN249 5.0 127.2 1.0 NH1 C:ARG96 5.0 127.2 1.0

N.P.D.Liau, M.C.Johnson, S.Izadi, L.Gerosa, M.Hammel, J.M.Bruning, T.J.Wendorff, W.Phung, S.G.Hymowitz, J.Sudhamsu. Structural Basis For SHOC2 Modulation of Ras Signalling. Nature V. 609 400 2022.
ISSN: ESSN 1476-4687
PubMed: 35768504
DOI: 10.1038/S41586-022-04838-3