Manganese in PDB 3dc6: Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans

All present enzymatic activity of Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans:
1.15.1.1;

The structure of Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans, PDB code: 3dc6 was solved by C.H.Trinh, T.Hunter, E.E.Stewart, S.E.V.Phillips, G.J.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.99 / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.980, 80.980, 137.444, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 20.1

The binding sites of Manganese atom in the Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans (pdb code 3dc6). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans, PDB code: 3dc6:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn198 b:8.7 occ:1.00 O A:HOH202 1.9 8.9 1.0 OD1 A:ASP158 2.0 8.1 1.0 NE2 A:HIS26 2.1 6.5 1.0 NE2 A:HIS74 2.2 8.9 1.0 NE2 A:HIS162 2.2 7.5 1.0 CG A:ASP158 3.0 8.2 1.0 CE1 A:HIS26 3.1 5.6 1.0 CE1 A:HIS74 3.1 9.0 1.0 CD2 A:HIS162 3.1 7.4 1.0 CD2 A:HIS74 3.1 8.7 1.0 CD2 A:HIS26 3.2 5.8 1.0 CE1 A:HIS162 3.2 7.1 1.0 OD2 A:ASP158 3.5 8.2 1.0 ND1 A:HIS74 4.2 9.6 1.0 ND1 A:HIS26 4.2 6.9 1.0 CZ2 A:TRP122 4.3 6.9 1.0 CG A:HIS74 4.3 9.4 1.0 CG A:HIS26 4.3 7.7 1.0 ND1 A:HIS162 4.3 6.7 1.0 CG A:HIS162 4.3 6.9 1.0 CB A:ASP158 4.3 7.6 1.0 NE2 A:GLN142 4.5 7.5 1.0 CB A:TRP160 4.5 6.4 1.0 CG A:TRP160 4.6 6.8 1.0 CH2 A:TRP122 4.9 7.8 1.0 CD1 A:TRP160 4.9 6.1 1.0 CB A:ALA163 4.9 7.3 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn198 b:18.8 occ:1.00 OD1 C:ASP158 2.0 15.3 1.0 O C:HOH220 2.1 14.2 1.0 NE2 C:HIS74 2.2 10.3 1.0 NE2 C:HIS162 2.2 13.4 1.0 NE2 C:HIS26 2.2 10.9 1.0 CG C:ASP158 3.1 15.2 1.0 CD2 C:HIS74 3.1 13.2 1.0 CE1 C:HIS74 3.1 12.9 1.0 CE1 C:HIS162 3.1 13.8 1.0 CD2 C:HIS162 3.2 13.9 1.0 CD2 C:HIS26 3.2 12.7 1.0 CE1 C:HIS26 3.2 13.0 1.0 OD2 C:ASP158 3.5 15.6 1.0 ND1 C:HIS74 4.2 11.6 1.0 ND1 C:HIS162 4.2 13.7 1.0 CG C:HIS74 4.2 12.8 1.0 CZ2 C:TRP122 4.3 14.8 1.0 CG C:HIS162 4.3 13.0 1.0 ND1 C:HIS26 4.3 11.3 1.0 CG C:HIS26 4.3 13.1 1.0 CB C:ASP158 4.3 15.8 1.0 NE2 C:GLN142 4.4 12.2 1.0 CB C:TRP160 4.5 13.1 1.0 CG C:TRP160 4.6 13.5 1.0 CD1 C:TRP160 4.8 14.3 1.0 CH2 C:TRP122 4.8 14.4 1.0 CB C:ALA163 4.9 14.4 1.0

C.H.Trinh, T.Hunter, E.E.Stewart, S.E.Phillips, G.J.Hunter. Purification, Crystallization and X-Ray Structures of the Two Manganese Superoxide Dismutases From Caenorhabditis Elegans Acta Crystallogr.,Sect.F V. 64 1110 2008.
ISSN: ESSN 1744-3091
PubMed: 19052361
DOI: 10.1107/S1744309108037056