Manganese in PDB 8gae: HSP90 Provides Platform For Craf Dephosphorylation By PP5

All present enzymatic activity of HSP90 Provides Platform For Craf Dephosphorylation By PP5:
2.7.11.1; 3.1.3.16;

The structure of HSP90 Provides Platform For Craf Dephosphorylation By PP5 also contains other interesting chemical elements:

Potassium	(K)	2 atoms
Magnesium	(Mg)	2 atoms

The binding sites of Manganese atom in the HSP90 Provides Platform For Craf Dephosphorylation By PP5 (pdb code 8gae). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the HSP90 Provides Platform For Craf Dephosphorylation By PP5, PDB code: 8gae:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the HSP90 Provides Platform For Craf Dephosphorylation By PP5


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of HSP90 Provides Platform For Craf Dephosphorylation By PP5 within 5.0Å range: probe atom residue distance (Å) B Occ E:Mn501 b:297.9 occ:1.00 OD1 E:ASP242 1.9 276.2 1.0 OD2 E:ASP271 2.0 276.3 1.0 NE2 E:HIS244 2.2 269.2 1.0 HH E:TYR451 2.9 253.4 1.0 HB2 E:ASP271 2.9 276.3 1.0 HE1 E:HIS244 2.9 269.2 1.0 CE1 E:HIS244 2.9 269.2 1.0 CG E:ASP242 3.0 276.2 1.0 CG E:ASP271 3.0 276.3 1.0 HE1 E:TYR451 3.2 253.4 1.0 MN E:MN502 3.4 282.4 1.0 HB3 E:ASP242 3.5 276.2 1.0 CD2 E:HIS244 3.5 269.2 1.0 CB E:ASP271 3.5 276.3 1.0 HB3 E:ASP271 3.6 276.3 1.0 HE1 E:PHE446 3.7 267.2 1.0 OD2 E:ASP242 3.7 276.2 1.0 CB E:ASP242 3.8 276.2 1.0 OH E:TYR451 3.8 253.4 1.0 HD2 E:HIS244 3.9 269.2 1.0 CE1 E:TYR451 4.1 253.4 1.0 O E:HIS427 4.1 259.3 1.0 OD1 E:ASP271 4.1 276.3 1.0 HB2 E:ASP242 4.2 276.2 1.0 ND1 E:HIS244 4.2 269.2 1.0 HZ E:PHE446 4.3 267.2 1.0 HA E:HIS427 4.3 259.3 1.0 HE1 E:HIS352 4.3 273.9 1.0 CZ E:TYR451 4.3 253.4 1.0 HB1 E:ALA304 4.4 274.3 1.0 HH21 E:ARG275 4.4 265.2 1.0 CG E:HIS244 4.5 269.2 1.0 H E:ASP271 4.5 276.3 1.0 CE1 E:PHE446 4.6 267.2 1.0 HB2 E:ALA304 4.7 274.3 1.0 CZ E:PHE446 4.8 267.2 1.0 CA E:ASP271 4.9 276.3 1.0 HH22 E:ARG275 4.9 265.2 1.0 C E:HIS427 5.0 259.3 1.0 NH2 E:ARG275 5.0 265.2 1.0 HD2 E:HIS427 5.0 259.3 1.0

Manganese binding site 2 out of 2 in the HSP90 Provides Platform For Craf Dephosphorylation By PP5


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of HSP90 Provides Platform For Craf Dephosphorylation By PP5 within 5.0Å range: probe atom residue distance (Å) B Occ E:Mn502 b:282.4 occ:1.00 OD2 E:ASP271 2.0 276.3 1.0 OD1 E:ASN303 2.0 274.0 1.0 HE2 E:HIS352 2.2 273.9 1.0 OD1 E:ASP271 2.5 276.3 1.0 CG E:ASP271 2.6 276.3 1.0 HE1 E:HIS352 2.7 273.9 1.0 NE2 E:HIS352 2.9 273.9 1.0 CE1 E:HIS352 3.1 273.9 1.0 CG E:ASN303 3.2 274.0 1.0 H E:ASN303 3.3 274.0 1.0 MN E:MN501 3.4 297.9 1.0 ND1 E:HIS427 3.4 259.3 1.0 CE1 E:HIS427 3.4 259.3 1.0 CG E:HIS427 3.4 259.3 1.0 HD22 E:ASN303 3.5 274.0 1.0 NE2 E:HIS427 3.5 259.3 1.0 CD2 E:HIS427 3.6 259.3 1.0 H E:ALA304 3.6 274.3 1.0 HA E:HIS427 3.7 259.3 1.0 ND2 E:ASN303 3.8 274.0 1.0 OD1 E:ASP242 3.8 276.2 1.0 HB1 E:ALA304 3.8 274.3 1.0 HD1 E:HIS427 3.9 259.3 1.0 HE1 E:HIS427 3.9 259.3 1.0 HE2 E:HIS427 4.0 259.3 1.0 CB E:ASP271 4.1 276.3 1.0 OD2 E:ASP242 4.1 276.2 1.0 HD2 E:HIS427 4.2 259.3 1.0 CD2 E:HIS352 4.2 273.9 1.0 N E:ASN303 4.2 274.0 1.0 CB E:HIS427 4.3 259.3 1.0 N E:ALA304 4.3 274.3 1.0 HB2 E:ASP271 4.3 276.3 1.0 CB E:ASN303 4.4 274.0 1.0 CG E:ASP242 4.4 276.2 1.0 ND1 E:HIS352 4.4 273.9 1.0 HB2 E:HIS427 4.4 259.3 1.0 HB2 E:ALA304 4.4 274.3 1.0 HB3 E:ASP271 4.4 276.3 1.0 CA E:HIS427 4.5 259.3 1.0 CB E:ALA304 4.6 274.3 1.0 O E:HIS427 4.6 259.3 1.0 HB3 E:ASN303 4.7 274.0 1.0 CA E:ASN303 4.7 274.0 1.0 HA3 E:GLY302 4.7 276.7 1.0 HD21 E:ASN303 4.8 274.0 1.0 HD2 E:HIS352 4.8 273.9 1.0 HE1 E:HIS244 4.8 269.2 1.0 HA2 E:GLY302 4.8 276.7 1.0 H E:ASP271 4.8 276.3 1.0 CG E:HIS352 4.9 273.9 1.0 C E:ASN303 5.0 274.0 1.0

M.Jaime-Garza, D.A.Agard, C.A.Nowotny, C.Coutandin, F.Wang, M.Tabios. HSP90 Provides A Platform For Kinase Dephosphorylation By PP5 Nat Commun 2023.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-023-37659-7