Manganese in PDB 3rva: Crystal Structure of Organophosphorus Acid Anhydrolase From Alteromonas Macleodii

All present enzymatic activity of Crystal Structure of Organophosphorus Acid Anhydrolase From Alteromonas Macleodii:
3.1.8.2; 3.4.13.9;

The structure of Crystal Structure of Organophosphorus Acid Anhydrolase From Alteromonas Macleodii, PDB code: 3rva was solved by A.Stepankova, T.Koval, L.H.Ostergaard, J.Duskova, T.Skalova, J.Hasek, J.Dohnalek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	133.770, 49.190, 97.340, 90.00, 125.03, 90.00
R / Rfree (%)	15.6 / n/a

The structure of Crystal Structure of Organophosphorus Acid Anhydrolase From Alteromonas Macleodii also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Manganese atom in the Crystal Structure of Organophosphorus Acid Anhydrolase From Alteromonas Macleodii (pdb code 3rva). 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 Organophosphorus Acid Anhydrolase From Alteromonas Macleodii, PDB code: 3rva:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Organophosphorus Acid Anhydrolase From Alteromonas Macleodii


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 Organophosphorus Acid Anhydrolase From Alteromonas Macleodii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn452 b:22.2 occ:0.70 OD1 A:ASP255 2.2 16.9 1.0 OE1 A:GLU423 2.3 16.9 1.0 O A:HOH460 2.3 15.4 0.5 OD2 A:ASP244 2.4 16.0 1.0 OD1 A:ASP244 2.4 16.1 1.0 O A:HOH857 2.5 30.1 1.0 CG A:ASP244 2.7 15.6 1.0 CG A:ASP255 3.1 17.1 1.0 CD A:GLU423 3.1 15.3 1.0 MN A:MN453 3.3 24.1 1.0 OE2 A:GLU423 3.3 16.3 1.0 OD2 A:ASP255 3.4 18.1 1.0 OG1 A:THR257 3.6 12.5 1.0 O A:HOH822 4.0 35.2 1.0 OH A:TYR212 4.0 15.8 1.0 O A:HOH459 4.0 20.8 0.5 CB A:ASP244 4.2 14.3 1.0 OE1 A:GLU384 4.3 23.3 1.0 CZ A:TYR212 4.4 16.1 1.0 CB A:ASP255 4.5 15.9 1.0 C A:ASP255 4.5 14.3 1.0 CE2 A:TYR212 4.5 16.4 1.0 CG A:GLU423 4.6 14.5 1.0 O A:ASP255 4.7 13.6 1.0 N A:ILE256 4.7 14.7 1.0 NE A:ARG421 4.7 15.1 1.0 NH2 A:ARG421 4.8 15.0 1.0 CA A:ASP255 4.9 14.7 1.0 CD A:GLU384 4.9 23.5 1.0 OE2 A:GLU384 4.9 23.4 1.0 O A:ILE256 4.9 12.9 1.0 C A:ILE256 5.0 13.3 1.0 CA A:ASP244 5.0 14.0 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Organophosphorus Acid Anhydrolase From Alteromonas Macleodii


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 Organophosphorus Acid Anhydrolase From Alteromonas Macleodii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn453 b:24.1 occ:1.00 OE2 A:GLU423 2.0 16.3 1.0 OD2 A:ASP255 2.2 18.1 1.0 NE2 A:HIS339 2.2 14.9 1.0 O A:HOH460 2.2 15.4 0.5 OE2 A:GLU384 2.6 23.4 1.0 O A:HOH459 3.1 20.8 0.5 CD A:GLU423 3.1 15.3 1.0 CG A:ASP255 3.1 17.1 1.0 CE1 A:HIS339 3.1 16.2 1.0 CD2 A:HIS339 3.2 15.7 1.0 MN A:MN452 3.3 22.2 0.7 OD1 A:ASP255 3.4 16.9 1.0 CD A:GLU384 3.4 23.5 1.0 OE1 A:GLU423 3.4 16.9 1.0 OE1 A:GLU384 3.6 23.3 1.0 CG2 A:THR382 3.7 13.7 1.0 OG1 A:THR382 3.7 14.5 1.0 CB A:THR382 4.0 14.3 1.0 O A:HOH857 4.1 30.1 1.0 ND1 A:HIS339 4.2 15.4 1.0 CG A:HIS339 4.3 14.3 1.0 CB A:ASP255 4.3 15.9 1.0 CG A:GLU423 4.4 14.5 1.0 CG A:GLU384 4.6 19.2 1.0 NE2 A:HIS346 4.8 25.3 1.0 O A:ASP255 4.9 13.6 1.0 CD2 A:HIS346 4.9 25.2 1.0

A.Stepankova, J.Duskova, T.Skalova, J.Hasek, T.Koval, L.H.Ostergaard, J.Dohnalek. Organophosphorus Acid Anhydrolase From Alteromonas Macleodii: Structural Study and Functional Relationship to Prolidases. Acta Crystallogr.,Sect.F V. 69 346 2013.
ISSN: ESSN 1744-3091
PubMed: 23545636
DOI: 10.1107/S1744309113002674