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Sodium in PDB 1k7e: Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Glycine Acid

Enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Glycine Acid

All present enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Glycine Acid:
4.2.1.20;

Protein crystallography data

The structure of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Glycine Acid, PDB code: 1k7e 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 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 182.651, 59.081, 67.300, 90.00, 94.55, 90.00
R / Rfree (%) 16.7 / 24.4

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Glycine Acid (pdb code 1k7e). 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 Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Glycine Acid, PDB code: 1k7e:

Sodium binding site 1 out of 1 in 1k7e

Go back to Sodium Binding Sites List in 1k7e
Sodium binding site 1 out of 1 in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Glycine Acid


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 Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Glycine Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na403

b:3.6
occ:1.00
 O B:HOH465 2.4 19.0 1.0
O B:SER308 2.4 12.8 1.0
O B:GLY232 2.4 13.5 1.0
O B:HOH466 2.5 21.9 1.0
O B:PHE306 2.6 23.7 1.0
C B:SER308 3.5 14.3 1.0
C B:GLY232 3.6 15.7 1.0
C B:PHE306 3.8 16.3 1.0
CG B:PRO270 3.9 13.2 1.0
N B:SER308 3.9 12.2 1.0
CD B:PRO270 3.9 9.9 1.0
CB B:PHE306 4.1 16.5 1.0
O B:GLY268 4.1 12.8 1.0
CA B:SER308 4.3 13.9 1.0
CA B:GLY232 4.3 9.0 1.0
CD2 B:PHE306 4.3 21.6 1.0
N B:VAL309 4.4 15.7 1.0
CA B:VAL309 4.4 9.5 1.0
CA B:PHE306 4.5 18.4 1.0
O B:VAL231 4.5 18.7 1.0
CB B:VAL309 4.5 11.1 1.0
C B:PRO307 4.5 15.1 1.0
OG B:SER297 4.6 22.1 1.0
CG B:PHE306 4.7 25.4 1.0
N B:PHE306 4.7 17.6 1.0
OE2 B:GLU256 4.7 22.8 1.0
N B:PRO307 4.7 15.8 1.0
N B:GLY233 4.7 12.3 1.0
CA B:GLY233 4.7 12.0 1.0
CA B:PRO307 4.8 16.5 1.0
CG2 B:VAL309 4.9 5.9 1.0

Reference:

M.Weyand, I.Schlichting, A.Marabotti, A.Mozzarelli. Crystal Structures of A New Class of Allosteric Effectors Complexed to Tryptophan Synthase. J.Biol.Chem. V. 277 10647 2002.
ISSN: ISSN 0021-9258
PubMed: 11756456
DOI: 10.1074/JBC.M111285200
Page generated: Sun Aug 17 05:45:26 2025

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