Sodium in PDB 4o53: Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370)

All present enzymatic activity of Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370):
5.3.1.1;

The structure of Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370), PDB code: 4o53 was solved by S.Lara-Gonzalez, G.M.Montero-Moran, P.Estrella-Hernandez, C.G.Benitez-Cardoza, L.G.Brieba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.40 / 2.00
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.891, 55.954, 105.157, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 22

The binding sites of Sodium atom in the Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370) (pdb code 4o53). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370), PDB code: 4o53:
Jump to Sodium binding site number: 1; 2; 3;

Sodium binding site 1 out of 3 in the Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370) within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:13.6 occ:1.00 O A:VAL227 2.3 11.8 1.0 O A:CYS224 2.3 13.3 1.0 O A:ALA222 2.4 12.7 1.0 OG A:SER251 2.4 14.1 1.0 O A:HOH560 2.5 24.4 1.0 CB A:SER251 3.5 16.1 1.0 C A:CYS224 3.5 14.1 1.0 C A:VAL227 3.5 14.7 1.0 C A:ALA222 3.5 12.8 1.0 CA A:SER251 4.1 17.3 1.0 O A:PRO225 4.1 13.2 1.0 C A:ALA223 4.1 21.4 1.0 N A:CYS224 4.1 13.0 1.0 N A:VAL227 4.1 13.0 1.0 CA A:VAL227 4.2 11.6 1.0 C A:PRO225 4.2 14.0 1.0 CB A:VAL227 4.3 11.8 1.0 CA A:PRO225 4.3 14.5 1.0 O A:ALA223 4.3 13.4 1.0 N A:PRO225 4.3 16.4 1.0 N A:ALA223 4.4 13.1 1.0 OXT A:LYS252 4.4 39.1 1.0 CA A:CYS224 4.4 16.7 1.0 CA A:ALA222 4.4 16.4 1.0 CA A:ALA223 4.4 18.3 1.0 N A:LYS252 4.5 24.2 1.0 CE1 A:PHE4 4.5 13.7 1.0 N A:ASP228 4.6 14.6 1.0 O A:LEU221 4.7 14.2 1.0 C A:SER251 4.7 22.8 1.0 O A:HOH489 4.8 23.9 1.0 CA A:ASP228 4.8 14.5 1.0 N A:ASP226 4.9 12.2 1.0 CG1 A:VAL227 4.9 11.7 1.0 CD1 A:PHE4 5.0 16.6 1.0

Sodium binding site 2 out of 3 in the Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370) within 5.0Å range: probe atom residue distance (Å) B Occ A:Na302 b:18.8 occ:1.00 O A:GLY156 2.2 25.0 1.0 O A:HOH555 2.3 42.2 1.0 O A:HOH557 2.3 28.9 1.0 OD1 A:ASP159 2.4 23.0 1.0 O A:HOH548 2.4 33.4 1.0 OD2 A:ASP159 2.5 31.6 1.0 CG A:ASP159 2.8 26.3 1.0 C A:GLY156 3.5 23.6 1.0 O A:HOH475 4.0 25.4 1.0 CB A:ASP159 4.2 22.9 1.0 CA A:LYS157 4.3 15.9 1.0 N A:LYS157 4.3 19.8 1.0 CA A:GLY156 4.4 24.8 1.0 OD2 A:ASP160 4.5 21.4 1.0 O A:HOH458 4.6 30.5 1.0 OD1 A:ASP160 4.8 14.9 1.0 CG A:ASP160 4.8 14.9 1.0 C A:LYS157 5.0 15.1 1.0

Sodium binding site 3 out of 3 in the Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Leu Mutant (TVAG_497370) within 5.0Å range: probe atom residue distance (Å) B Occ A:Na303 b:30.3 occ:1.00 O A:HOH513 2.4 29.7 1.0 O A:GLY136 2.4 20.7 1.0 O A:HOH571 2.5 31.4 1.0 O A:HOH554 2.5 34.4 1.0 C A:GLY136 3.6 22.2 1.0 CA A:GLY136 4.3 19.9 1.0 O A:HOH528 4.4 28.9 1.0 OE1 A:GLU140 4.5 23.8 1.0 OE2 A:GLU140 4.5 28.1 1.0 N A:LYS137 4.6 19.6 1.0 CD A:LYS137 4.8 28.8 1.0 CA A:LYS137 4.8 22.6 1.0 NZ A:LYS137 4.8 36.9 1.0 CD A:GLU140 5.0 25.7 1.0

S.Lara-Gonzalez, G.M.Montero-Moran, P.Estrella-Hernandez, C.G.Benitez-Cardoza, L.G.Brieba. Engineering Mutants with Altered Dimer-Monomer Equilibrium Reveal the Existence of Stable Monomeric Triosephosphate Isomerases To Be Published.