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Sodium in PDB 1k3u: Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Aspartic Acid

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

All present enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Aspartic 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]Aspartic Acid, PDB code: 1k3u 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 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 182.409, 59.718, 67.177, 90.00, 94.52, 90.00
R / Rfree (%) 15.3 / 18.8

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]Aspartic Acid (pdb code 1k3u). 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]Aspartic Acid, PDB code: 1k3u:

Sodium binding site 1 out of 1 in 1k3u

Go back to Sodium Binding Sites List in 1k3u
Sodium binding site 1 out of 1 in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with N- [1H-Indol-3-Yl-Acetyl]Aspartic 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]Aspartic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na803

b:14.3
occ:1.00
 O B:GLY232 2.3 14.4 1.0
O B:SER308 2.3 12.4 1.0
O B:HOH828 2.4 13.9 1.0
O B:HOH870 2.4 18.3 1.0
O B:PHE306 2.5 15.4 1.0
C B:GLY232 3.4 13.9 1.0
C B:SER308 3.5 11.9 1.0
C B:PHE306 3.6 14.9 1.0
CG B:PRO270 3.7 12.1 1.0
N B:SER308 3.9 13.3 1.0
CD B:PRO270 3.9 11.2 1.0
O B:GLY268 4.1 13.0 1.0
CA B:GLY232 4.1 11.3 1.0
CB B:PHE306 4.3 14.1 1.0
CA B:SER308 4.3 11.9 1.0
OG B:SER297 4.4 17.8 1.0
CA B:PHE306 4.4 14.8 1.0
O B:VAL231 4.4 10.5 1.0
CD2 B:PHE306 4.5 13.3 1.0
N B:GLY233 4.5 11.8 1.0
N B:VAL309 4.5 12.2 1.0
C B:PRO307 4.5 14.3 1.0
CA B:VAL309 4.6 10.6 1.0
N B:PRO307 4.6 13.8 1.0
N B:PHE306 4.6 15.4 1.0
CB B:VAL309 4.7 11.9 1.0
CA B:PRO307 4.7 13.6 1.0
CA B:GLY233 4.7 9.3 1.0
OE2 B:GLU256 4.8 12.2 1.0
CG B:PHE306 4.8 14.2 1.0
O B:LEU304 4.8 17.0 1.0
N B:GLY232 4.9 10.3 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 Oct 6 19:17:17 2024

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