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Sodium in PDB 1bks: Tryptophan Synthase (E.C.4.2.1.20) From Salmonella Typhimurium

Enzymatic activity of Tryptophan Synthase (E.C.4.2.1.20) From Salmonella Typhimurium

All present enzymatic activity of Tryptophan Synthase (E.C.4.2.1.20) From Salmonella Typhimurium:
4.2.1.20;

Protein crystallography data

The structure of Tryptophan Synthase (E.C.4.2.1.20) From Salmonella Typhimurium, PDB code: 1bks was solved by C.C.Hyde, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 184.580, 62.065, 67.610, 90.00, 94.69, 90.00
R / Rfree (%) n/a / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Tryptophan Synthase (E.C.4.2.1.20) From Salmonella Typhimurium (pdb code 1bks). 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 Tryptophan Synthase (E.C.4.2.1.20) From Salmonella Typhimurium, PDB code: 1bks:

Sodium binding site 1 out of 1 in 1bks

Go back to Sodium Binding Sites List in 1bks
Sodium binding site 1 out of 1 in the Tryptophan Synthase (E.C.4.2.1.20) From Salmonella Typhimurium


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Tryptophan Synthase (E.C.4.2.1.20) From Salmonella Typhimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na400

b:26.2
occ:1.00
O B:HOH402 2.2 21.5 0.9
O B:HOH403 2.3 22.6 1.0
O B:GLY232 2.3 21.6 1.0
O B:PHE306 2.5 33.1 1.0
O B:SER308 2.5 21.4 1.0
C B:GLY232 3.5 17.9 1.0
C B:PHE306 3.6 32.5 1.0
C B:SER308 3.7 19.3 1.0
CG B:PRO270 3.8 20.8 1.0
CD B:PRO270 3.9 24.6 1.0
O B:GLY268 4.0 16.0 1.0
N B:SER308 4.1 21.0 1.0
O B:VAL231 4.2 17.6 1.0
CA B:GLY232 4.2 13.7 1.0
CB B:PHE306 4.3 30.4 1.0
CA B:PHE306 4.3 31.4 1.0
CA B:SER308 4.5 20.6 1.0
N B:GLY233 4.5 16.4 1.0
N B:PHE306 4.5 32.0 1.0
O B:LEU304 4.6 32.3 1.0
CD2 B:PHE306 4.6 28.4 1.0
N B:VAL309 4.6 19.2 1.0
CB B:VAL309 4.6 19.9 1.0
N B:PRO307 4.7 31.7 1.0
OE2 B:GLU256 4.7 20.3 1.0
CA B:VAL309 4.7 15.9 1.0
OG B:SER297 4.7 42.9 1.0
C B:PRO307 4.7 25.7 1.0
CA B:GLY233 4.9 10.9 1.0
C B:VAL231 4.9 17.1 1.0
CG B:PHE306 4.9 25.8 1.0
CA B:PRO307 4.9 29.2 1.0
C B:GLY268 5.0 21.8 1.0
N B:GLY232 5.0 16.6 1.0
CG2 B:VAL309 5.0 20.9 1.0

Reference:

S.Rhee, K.D.Parris, S.A.Ahmed, E.W.Miles, D.R.Davies. Exchange of K+ or Cs+ For Na+ Induces Local and Long-Range Changes in the Three-Dimensional Structure of the Tryptophan Synthase ALPHA2BETA2 Complex. Biochemistry V. 35 4211 1996.
ISSN: ISSN 0006-2960
PubMed: 8672457
DOI: 10.1021/BI952506D
Page generated: Sun Oct 6 17:54:57 2024

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