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Sodium in PDB 1k8y: Crystal Structure of the Tryptophan Synthase Beta-SER178PRO Mutant Complexed with D,L-Alpha-Glycerol-3-Phosphate

Enzymatic activity of Crystal Structure of the Tryptophan Synthase Beta-SER178PRO Mutant Complexed with D,L-Alpha-Glycerol-3-Phosphate

All present enzymatic activity of Crystal Structure of the Tryptophan Synthase Beta-SER178PRO Mutant Complexed with D,L-Alpha-Glycerol-3-Phosphate:
4.2.1.20;

Protein crystallography data

The structure of Crystal Structure of the Tryptophan Synthase Beta-SER178PRO Mutant Complexed with D,L-Alpha-Glycerol-3-Phosphate, PDB code: 1k8y was solved by M.Weyand, I.Schlichting, A.Marabotti, A.Mozzarelli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.142, 60.465, 67.440, 90.00, 94.63, 90.00
R / Rfree (%) 17.1 / 20.9

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Tryptophan Synthase Beta-SER178PRO Mutant Complexed with D,L-Alpha-Glycerol-3-Phosphate (pdb code 1k8y). 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 the Tryptophan Synthase Beta-SER178PRO Mutant Complexed with D,L-Alpha-Glycerol-3-Phosphate, PDB code: 1k8y:

Sodium binding site 1 out of 1 in 1k8y

Go back to Sodium Binding Sites List in 1k8y
Sodium binding site 1 out of 1 in the Crystal Structure of the Tryptophan Synthase Beta-SER178PRO Mutant Complexed with D,L-Alpha-Glycerol-3-Phosphate


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 the Tryptophan Synthase Beta-SER178PRO Mutant Complexed with D,L-Alpha-Glycerol-3-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na703

b:15.6
occ:1.00
 O B:GLY232 2.2 16.5 1.0
O B:SER308 2.3 14.7 1.0
O B:HOH812 2.4 20.1 1.0
O B:HOH728 2.5 16.9 1.0
O B:PHE306 2.5 20.0 1.0
C B:GLY232 3.4 15.5 1.0
C B:SER308 3.5 15.6 1.0
C B:PHE306 3.7 17.1 1.0
CG B:PRO270 3.8 15.5 1.0
N B:SER308 4.0 16.9 1.0
CD B:PRO270 4.0 13.1 1.0
CA B:GLY232 4.1 13.4 1.0
O B:GLY268 4.1 14.9 1.0
CA B:SER308 4.4 15.0 1.0
OG B:SER297 4.4 22.3 1.0
CB B:PHE306 4.4 17.6 1.0
O B:VAL231 4.4 12.7 1.0
CA B:PHE306 4.4 19.2 1.0
N B:GLY233 4.5 14.2 1.0
CD2 B:PHE306 4.5 18.5 1.0
N B:VAL309 4.5 12.6 1.0
C B:PRO307 4.5 19.6 1.0
N B:PRO307 4.5 15.8 1.0
CA B:VAL309 4.6 12.8 1.0
N B:PHE306 4.7 18.2 1.0
CA B:PRO307 4.7 20.3 1.0
CB B:VAL309 4.7 12.6 1.0
O B:LEU304 4.8 20.9 1.0
CA B:GLY233 4.8 12.3 1.0
OE2 B:GLU256 4.9 15.7 1.0
CG B:PHE306 4.9 17.4 1.0
N B:GLY232 4.9 13.3 1.0

Reference:

M.Weyand, I.Schlichting, P.Herde, A.Marabotti, A.Mozzarelli. Crystal Structure of the Beta SER178--> Pro Mutant of Tryptophan Synthase. A "Knock-Out" Allosteric Enzyme. J.Biol.Chem. V. 277 10653 2002.
ISSN: ISSN 0021-9258
PubMed: 11756454
DOI: 10.1074/JBC.M111031200
Page generated: Sun Aug 17 05:45:46 2025

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