Manganese in PDB 1en5: Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant

All present enzymatic activity of Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant:
1.15.1.1;

The structure of Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant, PDB code: 1en5 was solved by R.A.Edwards, M.M.Whittaker, E.N.Baker, J.W.Whittaker, G.B.Jameson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	100.845, 108.893, 182.882, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 19.5

The binding sites of Manganese atom in the Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant (pdb code 1en5). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant, PDB code: 1en5:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:11.7 occ:1.00 OD2 A:ASP167 2.0 11.3 1.0 O A:HOH584 2.1 8.2 1.0 NE2 A:HIS26 2.2 10.6 1.0 NE2 A:HIS171 2.2 10.8 1.0 NE2 A:HIS81 2.2 14.3 1.0 CE1 A:HIS26 3.0 9.9 1.0 CE1 A:HIS171 3.1 8.6 1.0 CG A:ASP167 3.1 13.9 1.0 CE1 A:HIS81 3.1 13.1 1.0 CD2 A:HIS26 3.2 11.2 1.0 CD2 A:HIS81 3.2 12.3 1.0 CD2 A:HIS171 3.3 9.8 1.0 OD1 A:ASP167 3.5 14.0 1.0 ND1 A:HIS26 4.2 11.9 1.0 ND1 A:HIS171 4.2 10.1 1.0 ND1 A:HIS81 4.2 10.4 1.0 CG A:HIS26 4.3 12.0 1.0 CG A:HIS81 4.3 11.6 1.0 CB A:ASP167 4.3 12.8 1.0 CG A:HIS171 4.4 9.3 1.0 CZ2 A:TRP128 4.6 9.7 1.0 CB A:TRP169 4.7 6.2 1.0 NE2 A:GLN146 4.7 10.7 1.0 CG A:TRP169 4.8 8.9 1.0 CB A:ALA172 4.9 8.6 1.0

Manganese binding site 2 out of 4 in the Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:13.0 occ:1.00 OD2 B:ASP167 2.0 16.7 1.0 NE2 B:HIS26 2.1 13.0 1.0 O B:HOH567 2.2 11.5 1.0 NE2 B:HIS81 2.2 15.2 1.0 NE2 B:HIS171 2.3 14.6 1.0 CE1 B:HIS26 3.0 14.5 1.0 CG B:ASP167 3.0 16.5 1.0 CE1 B:HIS171 3.1 12.8 1.0 CE1 B:HIS81 3.1 14.2 1.0 CD2 B:HIS81 3.2 15.2 1.0 CD2 B:HIS26 3.2 15.3 1.0 CD2 B:HIS171 3.3 13.2 1.0 OD1 B:ASP167 3.5 16.4 1.0 ND1 B:HIS26 4.2 14.1 1.0 ND1 B:HIS81 4.2 14.0 1.0 CB B:ASP167 4.3 15.6 1.0 ND1 B:HIS171 4.3 12.9 1.0 CG B:HIS26 4.3 14.0 1.0 CG B:HIS81 4.3 15.1 1.0 CG B:HIS171 4.4 11.6 1.0 CZ2 B:TRP128 4.5 16.5 1.0 NE2 B:GLN146 4.7 12.3 1.0 CB B:TRP169 4.7 9.9 1.0 CG B:TRP169 4.9 11.1 1.0 CB B:ALA172 4.9 11.4 1.0

Manganese binding site 3 out of 4 in the Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn503 b:10.3 occ:1.00 OD2 C:ASP167 2.0 11.4 1.0 NE2 C:HIS26 2.2 7.8 1.0 NE2 C:HIS81 2.2 14.6 1.0 O C:HOH583 2.2 11.5 1.0 NE2 C:HIS171 2.3 11.7 1.0 CE1 C:HIS26 3.0 8.8 1.0 CG C:ASP167 3.1 10.8 1.0 CE1 C:HIS81 3.1 13.5 1.0 CD2 C:HIS81 3.1 13.5 1.0 CE1 C:HIS171 3.2 11.1 1.0 CD2 C:HIS26 3.2 6.9 1.0 CD2 C:HIS171 3.3 13.0 1.0 OD1 C:ASP167 3.6 11.9 1.0 ND1 C:HIS26 4.2 10.0 1.0 ND1 C:HIS81 4.2 11.8 1.0 CG C:HIS81 4.3 15.2 1.0 CG C:HIS26 4.3 8.6 1.0 CB C:ASP167 4.3 8.6 1.0 ND1 C:HIS171 4.3 12.3 1.0 CG C:HIS171 4.4 13.2 1.0 CZ2 C:TRP128 4.6 12.1 1.0 NE2 C:GLN146 4.7 13.4 1.0 CB C:TRP169 4.7 9.8 1.0 CG C:TRP169 4.9 11.9 1.0 CB C:ALA172 4.9 8.5 1.0

Manganese binding site 4 out of 4 in the Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure Analysis of the E. Coli Manganese Superoxide Dismutase Y34F Mutant within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn504 b:10.6 occ:1.00 OD2 D:ASP167 1.9 11.4 1.0 NE2 D:HIS26 2.2 11.3 1.0 NE2 D:HIS81 2.2 12.6 1.0 O D:HOH585 2.2 11.1 1.0 NE2 D:HIS171 2.3 7.2 1.0 CE1 D:HIS26 3.0 10.8 1.0 CG D:ASP167 3.0 14.1 1.0 CE1 D:HIS81 3.1 12.8 1.0 CE1 D:HIS171 3.2 8.3 1.0 CD2 D:HIS81 3.2 11.2 1.0 CD2 D:HIS26 3.2 8.7 1.0 CD2 D:HIS171 3.3 10.4 1.0 OD1 D:ASP167 3.5 13.4 1.0 ND1 D:HIS26 4.2 10.2 1.0 ND1 D:HIS81 4.2 12.3 1.0 CB D:ASP167 4.3 11.0 1.0 CG D:HIS26 4.3 11.4 1.0 CG D:HIS81 4.3 13.3 1.0 ND1 D:HIS171 4.3 6.4 1.0 CG D:HIS171 4.4 9.8 1.0 CZ2 D:TRP128 4.5 12.8 1.0 NE2 D:GLN146 4.6 11.1 1.0 CB D:TRP169 4.7 7.7 1.0 CG D:TRP169 4.9 9.6 1.0 CB D:ALA172 4.9 12.6 1.0

R.A.Edwards, M.M.Whittaker, J.W.Whittaker, E.N.Baker, G.B.Jameson. Outer Sphere Mutations Perturb Metal Reactivity in Manganese Superoxide Dismutase. Biochemistry V. 40 15 2001.
ISSN: ISSN 0006-2960
PubMed: 11141052
DOI: 10.1021/BI0018943