Sodium in PDB 5vwn: Triosephosphate Isomerases Deletion Loop 3 From Trichomonas Vaginalis

All present enzymatic activity of Triosephosphate Isomerases Deletion Loop 3 From Trichomonas Vaginalis:
5.3.1.1;

The structure of Triosephosphate Isomerases Deletion Loop 3 From Trichomonas Vaginalis, PDB code: 5vwn was solved by S.Lara-Gonzalez, K.Rojas-Mendez, P.Jimenez-Sandoval, P.Estrella-Hernandez, L.G.Brieba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.60 / 1.74
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.121, 57.030, 104.875, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 22.3

The binding sites of Sodium atom in the Triosephosphate Isomerases Deletion Loop 3 From Trichomonas Vaginalis (pdb code 5vwn). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Triosephosphate Isomerases Deletion Loop 3 From Trichomonas Vaginalis, PDB code: 5vwn:

Sodium binding site 1 out of 1 in the Triosephosphate Isomerases Deletion Loop 3 From Trichomonas Vaginalis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Triosephosphate Isomerases Deletion Loop 3 From Trichomonas Vaginalis within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:16.1 occ:1.00 O A:HOH452 2.3 26.1 1.0 O A:VAL221 2.3 13.8 1.0 O A:ALA216 2.4 15.4 1.0 O A:CYS218 2.4 17.3 1.0 OG A:SER245 2.4 16.0 1.0 CB A:SER245 3.5 16.6 1.0 C A:VAL221 3.5 17.4 1.0 C A:CYS218 3.5 14.7 1.0 C A:ALA216 3.5 15.9 1.0 CA A:SER245 4.1 15.4 1.0 C A:ALA217 4.1 18.1 1.0 N A:CYS218 4.1 13.4 1.0 N A:VAL221 4.1 13.5 1.0 CA A:VAL221 4.2 12.5 1.0 O A:PRO219 4.3 14.3 1.0 C A:PRO219 4.3 15.8 1.0 CA A:PRO219 4.3 16.1 1.0 O A:ALA217 4.4 18.6 1.0 CA A:CYS218 4.4 12.4 1.0 CB A:VAL221 4.4 15.9 1.0 N A:PRO219 4.4 13.5 1.0 CA A:ALA216 4.4 12.4 1.0 N A:ALA217 4.4 17.1 1.0 CA A:ALA217 4.5 17.0 1.0 N A:ASP222 4.5 13.7 1.0 CE1 A:PHE4 4.6 14.4 1.0 O A:HOH433 4.7 36.0 1.0 CA A:ASP222 4.7 12.5 1.0 O A:LEU215 4.8 14.6 1.0 C A:SER245 4.9 26.5 1.0 N A:ASP220 4.9 12.6 1.0 N A:LYS246 4.9 27.1 1.0

P.Jimenez-Sandoval, J.L.Vique-Sanchez, M.L.Hidalgo, G.Velazquez-Juarez, C.Diaz-Quezada, L.F.Arroyo-Navarro, G.M.Moran, J.Fattori, A.Jessica Diaz-Salazar, E.Rudino-Pinera, R.Sotelo-Mundo, A.C.M.Figueira, S.Lara-Gonzalez, C.G.Benitez-Cardoza, L.G.Brieba. A Competent Catalytic Active Site Is Necessary For Substrate Induced Dimer Assembly in Triosephosphate Isomerase. Biochim. Biophys. Acta V.1865 1423 2017.
ISSN: ISSN 0006-3002
PubMed: 28803140
DOI: 10.1016/J.BBAPAP.2017.07.014