Barium in PDB 4zwu: Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, V342L, I215Y

All present enzymatic activity of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, V342L, I215Y:
3.1.8.1; 3.1.8.2; 3.4.13.9;

The structure of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, V342L, I215Y, PDB code: 4zwu 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)	48.47 / 2.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.890, 68.846, 139.394, 90.00, 109.58, 90.00
R / Rfree (%)	17 / 21.9

The structure of Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, V342L, I215Y also contains other interesting chemical elements:

Manganese

(Mn)

6 atoms

The binding sites of Barium atom in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, V342L, I215Y (pdb code 4zwu). This binding sites where shown within 5.0 Angstroms radius around Barium atom.
In total 2 binding sites of Barium where determined in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, V342L, I215Y, PDB code: 4zwu:
Jump to Barium binding site number: 1; 2;

Barium binding site 1 out of 2 in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, V342L, I215Y


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, V342L, I215Y within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba503 b:60.3 occ:1.00 OD1 A:ASP29 2.8 60.2 1.0 O A:HOH772 2.8 64.2 1.0 OD2 A:ASP29 3.0 48.7 1.0 CG A:ASP29 3.2 55.9 1.0 MN A:MN504 4.2 0.8 1.0 CB A:ASP29 4.7 54.9 1.0

Barium binding site 2 out of 2 in the Crystal Structure of Organophosphate Anhydrolase/Prolidase Mutant Y212F, V342L, I215Y


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, V342L, I215Y within 5.0Å range: probe atom residue distance (Å) B Occ B:Ba506 b:0.5 occ:1.00 O B:HOH612 2.8 50.8 1.0 OD1 B:ASN27 2.9 77.3 1.0 O B:HOH753 3.2 65.5 1.0 CG B:ASN27 4.0 74.3 1.0 OE1 B:GLU24 4.7 93.7 1.0 ND2 B:ASN27 4.8 75.9 1.0 CB B:ASN27 4.9 69.9 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