Manganese in PDB 8avn: Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria

All present enzymatic activity of Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria:
1.15.1.1;

The structure of Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria, PDB code: 8avn was solved by A.Basle, A.Barwinska-Sendra, K.M.Sendra, K.Waldron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.49, 69.71, 58.01, 90, 100.24, 90
R / Rfree (%)	14.3 / 23.1

The binding sites of Manganese atom in the Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria (pdb code 8avn). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria, PDB code: 8avn:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:25.3 occ:1.00 OD2 A:ASP165 2.0 23.7 1.0 NE2 A:HIS82 2.2 21.9 1.0 NE2 A:HIS169 2.2 18.1 1.0 NE2 A:HIS27 2.2 21.4 1.0 O A:HOH470 2.3 22.5 1.0 CG A:ASP165 3.1 26.3 1.0 CD2 A:HIS82 3.1 24.7 1.0 CE1 A:HIS27 3.1 25.9 1.0 CD2 A:HIS169 3.1 17.6 1.0 CE1 A:HIS82 3.2 24.6 1.0 HD2 A:HIS82 3.2 23.7 1.0 CE1 A:HIS169 3.2 19.1 1.0 CD2 A:HIS27 3.2 21.8 1.0 HD2 A:HIS169 3.3 17.9 1.0 HE1 A:HIS27 3.3 22.9 1.0 HE1 A:HIS82 3.4 24.4 1.0 HE1 A:HIS169 3.4 18.3 1.0 HD2 A:HIS27 3.4 21.0 1.0 OD1 A:ASP165 3.5 22.7 1.0 HB2 A:TRP167 3.8 19.5 1.0 HZ2 A:TRP131 3.8 22.6 1.0 OH A:TYR35 4.1 45.1 1.0 HB2 A:ALA170 4.2 23.0 1.0 HE2 A:TYR35 4.2 36.8 1.0 ND1 A:HIS27 4.2 18.9 1.0 CG A:HIS82 4.3 24.2 1.0 ND1 A:HIS82 4.3 24.1 1.0 CG A:HIS169 4.3 18.5 1.0 ND1 A:HIS169 4.3 19.0 1.0 CB A:ASP165 4.3 22.5 1.0 CG A:HIS27 4.3 21.4 1.0 HB2 A:ASP165 4.4 22.3 1.0 CZ2 A:TRP131 4.5 22.8 1.0 HB3 A:HIS31 4.6 24.2 1.0 CB A:TRP167 4.6 19.2 1.0 HB3 A:ASP165 4.6 21.9 1.0 CG A:TRP167 4.7 20.6 1.0 HB3 A:TRP167 4.8 19.4 1.0 NE2 A:GLN150 4.8 33.3 1.0 HB2 A:HIS31 4.9 23.8 1.0 CE2 A:TYR35 4.9 35.5 1.0 CZ A:TYR35 4.9 35.4 1.0 HH2 A:TRP131 4.9 23.9 1.0

Manganese binding site 2 out of 2 in the Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Mutant of Superoxide Dismutase SODFM1 From Cpr Parcubacteria Wolfebacteria within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn301 b:25.3 occ:1.00 OD2 B:ASP165 2.0 28.7 1.0 O B:HOH423 2.1 22.2 1.0 NE2 B:HIS169 2.2 20.0 1.0 NE2 B:HIS27 2.2 21.4 1.0 NE2 B:HIS82 2.2 21.1 1.0 CG B:ASP165 3.0 25.1 1.0 CE1 B:HIS27 3.1 19.1 1.0 CD2 B:HIS169 3.1 22.9 1.0 CE1 B:HIS169 3.2 22.3 1.0 CD2 B:HIS82 3.2 22.5 1.0 HE1 B:HIS27 3.2 19.9 1.0 CE1 B:HIS82 3.2 28.6 1.0 HD2 B:HIS169 3.2 20.7 1.0 CD2 B:HIS27 3.3 22.2 1.0 HD2 B:HIS82 3.3 22.0 1.0 HE1 B:HIS169 3.4 21.7 1.0 HE1 B:HIS82 3.4 25.4 1.0 HD2 B:HIS27 3.5 22.0 1.0 OD1 B:ASP165 3.5 25.0 1.0 HB2 B:TRP167 3.7 19.2 1.0 HZ2 B:TRP131 3.9 23.9 1.0 OH B:TYR35 4.0 38.2 1.0 HB2 B:ALA170 4.1 21.9 1.0 ND1 B:HIS27 4.2 23.3 1.0 HE2 B:TYR35 4.3 32.1 1.0 ND1 B:HIS169 4.3 20.5 1.0 CG B:HIS169 4.3 18.7 1.0 CG B:HIS82 4.3 21.7 1.0 CB B:ASP165 4.3 22.4 1.0 ND1 B:HIS82 4.3 23.9 1.0 CG B:HIS27 4.3 20.7 1.0 HB2 B:ASP165 4.4 22.7 1.0 CZ2 B:TRP131 4.5 22.5 1.0 HB3 B:ASP165 4.5 22.5 1.0 HB3 B:HIS31 4.5 24.6 1.0 CB B:TRP167 4.6 19.1 1.0 CG B:TRP167 4.7 20.5 1.0 HB3 B:TRP167 4.8 19.4 1.0 NE2 B:GLN150 4.8 31.7 1.0 HH2 B:TRP131 4.9 25.4 1.0 CE2 B:TYR35 4.9 31.8 1.0 CZ B:TYR35 5.0 31.2 1.0 HB2 B:HIS31 5.0 25.2 1.0

K.M.Sendra, A.Barwinska-Sendra, E.S.Mackenzie, A.Basle, T.E.Kehl-Fie, K.J.Waldron. An Ancient Metalloenzyme Evolves Through Metal Preference Modulation. Nat Ecol Evol 2023.
ISSN: ISSN 2397-334X
PubMed: 37037909
DOI: 10.1038/S41559-023-02012-0