Arsenic in PDB 5byk: Schistosoma Mansoni (Blood Fluke) Sulfotransferase/S-Oxamniquine Complex

The structure of Schistosoma Mansoni (Blood Fluke) Sulfotransferase/S-Oxamniquine Complex, PDB code: 5byk was solved by A.B.Taylor, X.Cao, S.P.Holloway, P.J.Hart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.41 / 1.28
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	140.587, 39.433, 54.003, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 17.1

The structure of Schistosoma Mansoni (Blood Fluke) Sulfotransferase/S-Oxamniquine Complex also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Arsenic atom in the Schistosoma Mansoni (Blood Fluke) Sulfotransferase/S-Oxamniquine Complex (pdb code 5byk). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Schistosoma Mansoni (Blood Fluke) Sulfotransferase/S-Oxamniquine Complex, PDB code: 5byk:

Arsenic binding site 1 out of 1 in the Schistosoma Mansoni (Blood Fluke) Sulfotransferase/S-Oxamniquine Complex


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Schistosoma Mansoni (Blood Fluke) Sulfotransferase/S-Oxamniquine Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:As226 b:26.5 occ:0.55 AS A:CAS226 0.0 26.5 0.6 CE2 A:CAS226 2.0 28.7 0.6 CE1 A:CAS226 2.0 25.0 0.6 SG A:CAS226 2.3 28.2 1.0 O A:CAS226 3.2 20.9 1.0 CB A:CAS226 3.2 18.9 1.0 C A:CAS226 3.6 17.4 1.0 O A:HOH690 4.0 45.8 1.0 CA A:CAS226 4.0 16.9 1.0 N A:VAL227 4.4 15.8 1.0 CA A:VAL227 4.9 15.2 1.0

A.B.Taylor, L.Pica-Mattoccia, C.M.Polcaro, E.Donati, X.Cao, A.Basso, A.Guidi, A.R.Rugel, S.P.Holloway, T.J.Anderson, P.J.Hart, D.Cioli, P.T.Loverde. Structural and Functional Characterization of the Enantiomers of the Antischistosomal Drug Oxamniquine. Plos Negl Trop Dis V. 9 04132 2015.
ISSN: ESSN 1935-2735
PubMed: 26485649
DOI: 10.1371/JOURNAL.PNTD.0004132