Manganese in PDB 8vhw: Neutron Structure of Peroxide-Soaked TRP161PHE Mnsod

All present enzymatic activity of Neutron Structure of Peroxide-Soaked TRP161PHE Mnsod:
1.15.1.1;

The binding sites of Manganese atom in the Neutron Structure of Peroxide-Soaked TRP161PHE Mnsod (pdb code 8vhw). 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 TRP161PHE Mnsod, PDB code: 8vhw:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Neutron Structure of Peroxide-Soaked TRP161PHE 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 TRP161PHE Mnsod within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:19.6 occ:1.00 O A:HOH336 2.1 19.2 1.0 NE2 A:HIS74 2.1 19.2 1.0 NE2 A:HIS26 2.1 18.8 1.0 OD2 A:ASP159 2.2 19.4 1.0 NE2 A:HIS163 2.2 19.1 1.0 D1 A:HOH336 2.3 23.0 1.0 D2 A:HOH336 2.5 23.0 1.0 CE1 A:HIS74 3.1 19.1 1.0 CE1 A:HIS26 3.1 17.9 1.0 CD2 A:HIS74 3.1 19.5 1.0 CD2 A:HIS26 3.1 18.7 1.0 CE1 A:HIS163 3.2 19.0 1.0 CD2 A:HIS163 3.3 19.4 1.0 CG A:ASP159 3.3 19.4 1.0 DE1 A:HIS74 3.3 22.9 1.0 DE1 A:HIS163 3.3 22.8 1.0 DE1 A:HIS26 3.3 21.5 1.0 DD2 A:HIS26 3.3 22.4 1.0 DD2 A:HIS74 3.3 23.4 1.0 DD2 A:HIS163 3.5 23.2 1.0 DB2 A:PHE161 3.5 23.3 1.0 DZ2 A:TRP123 3.6 23.3 1.0 OD1 A:ASP159 3.8 19.3 1.0 DE2 A:TYR34 3.8 23.1 1.0 ND1 A:HIS74 4.2 18.1 1.0 ND1 A:HIS26 4.2 18.5 1.0 CG A:HIS74 4.2 18.8 1.0 CG A:HIS26 4.2 18.9 1.0 DH A:TYR34 4.2 24.7 1.0 DB3 A:ALA164 4.3 23.1 1.0 ND1 A:HIS163 4.3 19.2 1.0 CZ2 A:TRP123 4.3 19.4 1.0 CB A:PHE161 4.3 19.4 1.0 NE2 A:GLN143 4.4 18.8 1.0 CG A:HIS163 4.4 19.0 1.0 DB3 A:PHE161 4.5 23.3 1.0 DB3 A:HIS30 4.5 23.8 1.0 CG A:PHE161 4.5 19.5 1.0 CB A:ASP159 4.6 19.0 1.0 DB2 A:ASP159 4.7 22.8 1.0 DH2 A:TRP123 4.7 23.6 1.0 DB3 A:ASP159 4.8 22.8 1.0 CD1 A:PHE161 4.8 20.0 1.0 CE2 A:TYR34 4.9 19.2 1.0 CH2 A:TRP123 4.9 19.7 1.0 DE21 A:GLN143 4.9 22.6 1.0 DD1 A:PHE161 4.9 24.0 1.0 OH A:TYR34 4.9 20.6 1.0 CD2 A:PHE161 4.9 19.4 1.0 DB2 A:HIS30 5.0 23.8 1.0

Manganese binding site 2 out of 2 in the Neutron Structure of Peroxide-Soaked TRP161PHE 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 TRP161PHE Mnsod within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:19.2 occ:1.00 O2 B:PEO202 2.0 18.9 1.0 OD2 B:ASP159 2.1 19.1 1.0 NE2 B:HIS26 2.1 20.0 1.0 NE2 B:HIS163 2.1 18.7 1.0 NE2 B:HIS74 2.3 20.2 1.0 O1 B:PEO202 2.6 19.5 1.0 CE1 B:HIS26 3.0 19.9 1.0 CE1 B:HIS163 3.1 19.1 1.0 CD2 B:HIS26 3.1 19.9 1.0 CD2 B:HIS163 3.2 19.3 1.0 CE1 B:HIS74 3.2 19.1 1.0 CG B:ASP159 3.2 19.0 1.0 CD2 B:HIS74 3.2 20.6 1.0 DE1 B:HIS26 3.2 23.9 1.0 DE1 B:HIS163 3.3 22.9 1.0 DE22 B:GLN143 3.3 22.6 1.0 DD2 B:HIS26 3.4 23.8 1.0 DE1 B:HIS74 3.4 22.9 1.0 DB2 B:PHE161 3.4 22.9 1.0 DD2 B:HIS163 3.4 23.1 1.0 DD2 B:HIS74 3.5 24.7 1.0 DO1 B:PEO202 3.5 23.4 1.0 OD1 B:ASP159 3.7 19.2 1.0 DZ2 B:TRP123 3.7 22.9 1.0 DE2 B:TYR34 4.0 24.5 1.0 ND1 B:HIS26 4.1 19.4 1.0 CG B:HIS26 4.2 19.9 1.0 CB B:PHE161 4.2 19.1 1.0 ND1 B:HIS163 4.2 20.1 1.0 ND1 B:HIS74 4.3 19.6 1.0 DB2 B:ALA164 4.3 22.8 1.0 CG B:HIS163 4.3 18.3 1.0 NE2 B:GLN143 4.3 19.6 1.0 DB3 B:PHE161 4.3 22.9 1.0 CG B:HIS74 4.3 19.9 1.0 CB B:ASP159 4.4 18.9 1.0 CG B:PHE161 4.5 19.1 1.0 CZ2 B:TRP123 4.5 19.1 1.0 DB3 B:HIS30 4.5 24.1 1.0 DB2 B:ASP159 4.5 22.6 1.0 DB3 B:ASP159 4.7 22.6 1.0 CD1 B:PHE161 4.7 18.9 1.0 DD1 B:PHE161 4.7 22.7 1.0 OH B:TYR34 4.8 19.3 1.0 DO1 B:PEO203 4.8 24.5 1.0 DE21 B:GLN143 4.9 23.5 1.0 HE1 B:TRP123 4.9 23.6 0.3 DE1 B:TRP123 4.9 23.4 0.7 D B:PHE161 4.9 23.3 1.0 CE2 B:TYR34 5.0 20.4 1.0 DB3 B:ALA164 5.0 22.8 1.0

J.Azadmanesh, K.Slobodnik, L.R.Struble, W.E.Lutz, L.Coates, K.L.Weiss, D.A.A.Myles, T.Kroll, G.E.O.Borgstahl. Revealing the Atomic and Electronic Mechanism of Human Manganese Superoxide Dismutase Product Inhibition. Biorxiv 2024.
ISSN: ISSN 2692-8205
PubMed: 38328249
DOI: 10.1101/2024.01.26.577433