Manganese in PDB 9bvy: Neutron Structure of Peroxide-Soaked TYR34PHE Mnsod

All present enzymatic activity of Neutron Structure of Peroxide-Soaked TYR34PHE Mnsod:
1.15.1.1;

The binding sites of Manganese atom in the Neutron Structure of Peroxide-Soaked TYR34PHE Mnsod (pdb code 9bvy). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Neutron Structure of Peroxide-Soaked TYR34PHE Mnsod, PDB code: 9bvy:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Neutron Structure of Peroxide-Soaked TYR34PHE Mnsod


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Neutron Structure of Peroxide-Soaked TYR34PHE Mnsod within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:2.9 occ:1.00 O2 A:PEO202 2.0 2.8 1.0 OD2 A:ASP159 2.1 3.1 1.0 NE2 A:HIS26 2.2 2.9 1.0 NE2 A:HIS163 2.2 2.5 1.0 NE2 A:HIS74 2.2 2.7 1.0 O1 A:PEO202 2.3 2.8 1.0 CE1 A:HIS163 2.9 2.2 1.0 DE1 A:HIS163 3.0 3.4 1.0 CE1 A:HIS74 3.0 2.5 1.0 CE1 A:HIS26 3.1 2.8 1.0 DE1 A:HIS74 3.1 2.9 1.0 CD2 A:HIS26 3.1 2.7 1.0 CG A:ASP159 3.3 3.4 1.0 DO1 A:PEO202 3.3 3.4 1.0 DE1 A:HIS26 3.3 3.3 1.0 CD2 A:HIS74 3.3 2.4 1.0 CD2 A:HIS163 3.4 2.6 1.0 DD2 A:HIS26 3.4 3.3 1.0 DB2 A:TRP161 3.4 3.2 1.0 DE22 A:GLN143 3.6 2.7 1.0 DZ2 A:TRP123 3.7 3.4 1.0 DD2 A:HIS74 3.7 2.9 1.0 OD1 A:ASP159 3.7 3.2 1.0 DD2 A:HIS163 3.8 3.1 1.0 ND1 A:HIS26 4.1 2.6 1.0 ND1 A:HIS163 4.2 3.0 1.0 DE2 A:PHE34 4.2 2.4 1.0 ND1 A:HIS74 4.2 2.4 1.0 CG A:HIS26 4.2 2.9 1.0 CB A:TRP161 4.2 2.7 1.0 CG A:TRP161 4.4 2.7 1.0 CG A:HIS74 4.4 2.4 1.0 CZ2 A:TRP123 4.4 2.8 1.0 CG A:HIS163 4.4 2.9 1.0 DB3 A:TRP161 4.4 3.2 1.0 CB A:ASP159 4.5 3.4 1.0 NE2 A:GLN143 4.6 2.3 1.0 DB3 A:HIS30 4.6 3.1 1.0 DB3 A:ALA164 4.6 4.0 1.0 DB2 A:ASP159 4.6 4.1 1.0 DB2 A:ALA164 4.7 4.0 1.0 CD1 A:TRP161 4.7 2.7 1.0 DB3 A:ASP159 4.7 4.1 1.0 DH2 A:TRP123 4.8 3.6 1.0 CD2 A:TRP161 4.8 2.4 1.0 DD1 A:TRP161 4.9 3.2 1.0 CH2 A:TRP123 5.0 3.0 1.0 DB2 A:HIS30 5.0 3.1 1.0 DE21 A:GLN143 5.0 2.7 1.0

Manganese binding site 2 out of 2 in the Neutron Structure of Peroxide-Soaked TYR34PHE Mnsod


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Neutron Structure of Peroxide-Soaked TYR34PHE Mnsod within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:1.9 occ:1.00 O B:HOH365 1.8 1.8 1.0 O B:HOH301 1.8 1.9 1.0 OD2 B:ASP159 2.0 1.8 1.0 NE2 B:HIS26 2.1 1.8 1.0 NE2 B:HIS74 2.2 2.1 1.0 NE2 B:HIS163 2.2 1.9 1.0 D1 B:HOH365 2.2 2.1 1.0 D1 B:HOH301 2.3 2.3 1.0 CE1 B:HIS26 2.9 2.1 1.0 CE1 B:HIS163 2.9 1.8 1.0 DE1 B:HIS163 3.0 2.2 1.0 CD2 B:HIS74 3.0 2.0 1.0 DE1 B:HIS26 3.1 2.5 1.0 CG B:ASP159 3.2 1.9 1.0 CD2 B:HIS26 3.2 1.9 1.0 CE1 B:HIS74 3.2 2.2 1.0 DD2 B:HIS74 3.2 2.4 1.0 DE22 B:GLN143 3.3 2.0 0.5 HE22 B:GLN143 3.3 2.0 0.5 CD2 B:HIS163 3.4 2.2 1.0 DZ2 B:TRP123 3.4 2.2 1.0 DE1 B:HIS74 3.5 2.6 1.0 DD2 B:HIS26 3.5 2.2 1.0 DB2 B:TRP161 3.5 2.2 1.0 OD1 B:ASP159 3.7 1.8 1.0 DD2 B:HIS163 3.7 2.6 1.0 CZ2 B:TRP123 4.1 1.9 1.0 ND1 B:HIS26 4.1 2.2 1.0 DB2 B:ALA164 4.1 2.4 1.0 ND1 B:HIS163 4.2 1.9 1.0 CG B:HIS74 4.2 1.9 1.0 DE2 B:PHE34 4.2 2.5 1.0 CG B:HIS26 4.2 1.9 1.0 ND1 B:HIS74 4.2 1.9 1.0 NE2 B:GLN143 4.3 1.7 1.0 CB B:TRP161 4.4 1.8 1.0 CG B:HIS163 4.4 1.9 1.0 CB B:ASP159 4.4 2.1 1.0 CG B:TRP161 4.5 1.6 1.0 DH2 B:TRP123 4.5 2.2 1.0 DB2 B:ASP159 4.5 2.5 1.0 DB3 B:TRP161 4.6 2.2 1.0 DB3 B:HIS30 4.6 2.5 1.0 CH2 B:TRP123 4.6 1.8 1.0 DB3 B:ASP159 4.7 2.5 1.0 CD1 B:TRP161 4.7 1.6 1.0 DE21 B:GLN143 4.8 2.0 0.7 HE21 B:GLN143 4.8 2.0 0.3 HE1 B:TRP123 4.8 2.1 0.5 DE1 B:TRP123 4.8 2.1 0.5 CE2 B:TRP123 4.9 2.0 1.0 DD1 B:TRP161 4.9 1.9 1.0 CD2 B:TRP161 4.9 1.6 1.0 DD1 B:HIS26 5.0 2.6 1.0

J.Azadmanesh, K.Slobodnik, L.R.Struble, J.J.Lovelace, E.A.Cone, M.Dasgupta, W.E.Lutz, S.Kumar, A.Natarajan, L.Coates, K.L.Weiss, D.A.A.Myles, T.Kroll, G.E.O.Borgstahl. The Role of TYR34 in Proton Coupled Electron Transfer and Product Inhibition of Manganese Superoxide Dismutase. Nat Commun V. 16 1887 2025.
ISSN: ESSN 2041-1723
PubMed: 39987263
DOI: 10.1038/S41467-025-57180-3