Barium in PDB 4zwp: Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F

All present enzymatic activity of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F:
3.4.13.9;

The structure of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, PDB code: 4zwp was solved by C.M.Daczkowski, S.D.Pegan, S.P.Harvey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.94 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	104.493, 68.179, 142.479, 90.00, 110.50, 90.00
R / Rfree (%)	17.3 / 22.6

The structure of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F also contains other interesting chemical elements:

Manganese

(Mn)

7 atoms

The binding sites of Barium atom in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F (pdb code 4zwp). This binding sites where shown within 5.0 Angstroms radius around Barium atom.
In total 3 binding sites of Barium where determined in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, PDB code: 4zwp:
Jump to Barium binding site number: 1; 2; 3;

Barium binding site 1 out of 3 in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 1 of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba503 b:0.2 occ:0.50 O A:HOH781 2.9 47.1 0.5 OD1 A:ASP318 3.7 58.2 1.0 OD2 A:ASP318 3.7 60.6 1.0 CG A:ASP318 4.1 59.0 1.0 O A:HOH687 4.8 39.8 1.0 OE1 A:GLN301 4.8 53.3 1.0 NE2 A:GLN301 4.9 50.3 1.0 CD A:GLN301 5.0 50.5 1.0

Barium binding site 2 out of 3 in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 2 of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba506 b:0.2 occ:1.00 O A:ASP309 2.9 48.4 1.0 OD1 A:ASN311 4.0 49.0 1.0 C A:ASP309 4.0 45.6 1.0 BA A:BA507 4.5 0.8 1.0 O A:HOH756 4.6 48.3 1.0 CA A:ASP309 4.8 45.1 1.0 CA A:PHE310 4.9 42.3 1.0 N A:PHE310 4.9 43.4 1.0

Barium binding site 3 out of 3 in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 3 of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba507 b:0.8 occ:1.00 O A:HOH729 2.7 64.0 1.0 OE1 A:GLU267 4.2 58.5 1.0 BA A:BA506 4.5 0.2 1.0 CD A:GLU267 4.7 55.1 1.0 OE1 A:GLU270 4.9 51.8 1.0

C.M.Daczkowski, S.D.Pegan, S.P.Harvey. Engineering the Organophosphorus Acid Anhydrolase Enzyme For Increased Catalytic Efficiency and Broadened Stereospecificity on Russian Vx. Biochemistry V. 54 6423 2015.
ISSN: ISSN 0006-2960
PubMed: 26418828
DOI: 10.1021/ACS.BIOCHEM.5B00624