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Sodium in PDB 4o57: Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Tyr Mutant (TVAG_497370)

Enzymatic activity of Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Tyr Mutant (TVAG_497370)

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

Protein crystallography data

The structure of Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Tyr Mutant (TVAG_497370), PDB code: 4o57 was solved by S.Lara-Gonzalez, P.Estrella-Hernandez, G.M.Montero-Moran, 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) 35.33 / 1.79
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.285, 56.346, 106.308, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Tyr Mutant (TVAG_497370) (pdb code 4o57). 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 Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Tyr Mutant (TVAG_497370), PDB code: 4o57:

Sodium binding site 1 out of 1 in 4o57

Go back to Sodium Binding Sites List in 4o57
Sodium binding site 1 out of 1 in the Crystal Structure of Trichomonas Vaginalis Triosephosphate Isomerase ILE45-Tyr 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-Tyr Mutant (TVAG_497370) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:18.5
occ:1.00
 O A:ALA222 2.3 19.9 1.0
O A:HOH412 2.3 29.1 1.0
O A:VAL227 2.3 20.5 1.0
O A:CSO224 2.3 18.6 1.0
O A:HOH475 2.4 38.9 1.0
OG A:SER251 2.5 21.8 1.0
C A:CSO224 3.5 20.4 1.0
C A:ALA222 3.5 17.3 1.0
CB A:SER251 3.5 20.8 1.0
HA A:SER251 3.5 22.4 1.0
C A:VAL227 3.5 17.1 1.0
HB2 A:SER251 3.5 25.0 1.0
HB A:VAL227 3.7 22.5 1.0
HE1 A:PHE4 3.7 21.3 1.0
H A:VAL227 3.8 21.8 1.0
HA A:PRO225 3.8 21.8 1.0
N A:CSO224 4.0 18.3 1.0
C A:ALA223 4.0 22.7 1.0
CA A:SER251 4.0 18.7 1.0
HA A:ASP228 4.1 20.1 1.0
HA A:ALA222 4.1 20.1 1.0
HA A:ALA223 4.2 26.1 1.0
H A:CSO224 4.2 21.9 1.0
N A:VAL227 4.2 18.2 1.0
CA A:VAL227 4.2 17.6 1.0
O A:PRO225 4.2 18.2 1.0
C A:PRO225 4.3 16.8 1.0
CA A:PRO225 4.3 18.1 1.0
HB3 A:SER251 4.3 25.0 1.0
H A:LYS252 4.3 37.3 1.0
CA A:CSO224 4.3 21.6 1.0
O A:ALA223 4.3 19.2 1.0
N A:ALA223 4.3 19.1 1.0
O A:HOH489 4.4 45.1 1.0
N A:PRO225 4.4 19.7 1.0
CB A:VAL227 4.4 18.8 1.0
CA A:ALA223 4.4 21.8 1.0
CA A:ALA222 4.4 16.8 1.0
N A:ASP228 4.5 16.2 1.0
HB3 A:CSO224 4.5 24.5 1.0
HD1 A:PHE4 4.6 24.3 1.0
CE1 A:PHE4 4.6 17.8 1.0
HG12 A:VAL227 4.6 26.7 1.0
C A:SER251 4.7 27.0 1.0
O A:LEU221 4.7 20.6 1.0
N A:LYS252 4.8 31.1 1.0
CA A:ASP228 4.8 16.7 1.0
O A:HOH442 4.8 37.1 1.0
HB1 A:ALA222 4.9 21.6 1.0
N A:ASP226 4.9 14.6 1.0
CB A:CSO224 5.0 20.4 1.0

Reference:

S.Lara-Gonzalez, P.Estrella-Hernandez, G.M.Montero-Moran, 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.
Page generated: Mon Oct 7 17:24:39 2024

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