Manganese in PDB 3dc5: 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: 3dc5 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)	44.07 / 1.70
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.780, 81.780, 136.031, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 22.6

The binding sites of Manganese atom in the Crystal Structure of A Manganese Superoxide Dismutases From Caenorhabditis Elegans (pdb code 3dc5). 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: 3dc5:
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:Mn195 b:13.7 occ:1.00 OD1 A:ASP155 2.1 15.4 1.0 NE2 A:HIS74 2.2 12.2 1.0 NE2 A:HIS159 2.2 10.7 1.0 NE2 A:HIS26 2.2 10.7 1.0 O A:HOH197 2.3 9.9 1.0 CD2 A:HIS74 3.0 14.4 1.0 CG A:ASP155 3.1 10.8 1.0 CD2 A:HIS159 3.1 12.2 1.0 CE1 A:HIS26 3.2 12.8 1.0 CD2 A:HIS26 3.2 11.0 1.0 CE1 A:HIS74 3.2 14.3 1.0 CE1 A:HIS159 3.2 12.2 1.0 OD2 A:ASP155 3.4 12.6 1.0 CG A:HIS74 4.2 13.5 1.0 ND1 A:HIS74 4.3 13.3 1.0 CZ2 A:TRP122 4.3 14.0 1.0 CG A:HIS159 4.3 9.6 1.0 ND1 A:HIS26 4.3 12.1 1.0 ND1 A:HIS159 4.3 12.7 1.0 CG A:HIS26 4.4 11.8 1.0 CB A:ASP155 4.4 13.7 1.0 CB A:TRP157 4.5 13.8 1.0 NE2 A:GLN142 4.6 13.2 1.0 CG A:TRP157 4.7 12.8 1.0 CH2 A:TRP122 4.8 15.1 1.0 CB A:ALA160 4.9 12.4 1.0 CD1 A:TRP157 5.0 13.1 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:Mn195 b:16.1 occ:1.00 OD1 C:ASP155 2.1 16.0 1.0 NE2 C:HIS159 2.1 12.0 1.0 NE2 C:HIS74 2.2 13.9 1.0 NE2 C:HIS26 2.2 12.7 1.0 O C:HOH196 2.3 11.8 1.0 CD2 C:HIS159 3.1 12.6 1.0 CE1 C:HIS159 3.1 14.7 1.0 CG C:ASP155 3.1 15.2 1.0 CE1 C:HIS74 3.2 17.3 1.0 CD2 C:HIS74 3.2 15.3 1.0 CE1 C:HIS26 3.2 16.6 1.0 CD2 C:HIS26 3.2 15.9 1.0 OD2 C:ASP155 3.6 13.3 1.0 ND1 C:HIS159 4.2 15.9 1.0 CG C:HIS159 4.2 14.2 1.0 ND1 C:HIS74 4.3 17.1 1.0 ND1 C:HIS26 4.3 16.8 1.0 CG C:HIS74 4.3 16.3 1.0 CG C:HIS26 4.3 15.4 1.0 CZ2 C:TRP122 4.4 14.4 1.0 CB C:ASP155 4.4 14.5 1.0 CB C:TRP157 4.5 13.6 1.0 NE2 C:GLN142 4.5 14.7 1.0 CG C:TRP157 4.6 12.9 1.0 CB C:ALA160 4.9 15.1 1.0 CH2 C:TRP122 4.9 15.8 1.0 CD1 C:TRP157 5.0 14.9 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