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Sodium in PDB 2clo: Tryptophan Synthase (External Aldimine State) in Complex with (Naphthalene-2'-Sulfonyl)-2-Amino-1-Ethylphosphate (F19)

Enzymatic activity of Tryptophan Synthase (External Aldimine State) in Complex with (Naphthalene-2'-Sulfonyl)-2-Amino-1-Ethylphosphate (F19)

All present enzymatic activity of Tryptophan Synthase (External Aldimine State) in Complex with (Naphthalene-2'-Sulfonyl)-2-Amino-1-Ethylphosphate (F19):
4.2.1.20;

Protein crystallography data

The structure of Tryptophan Synthase (External Aldimine State) in Complex with (Naphthalene-2'-Sulfonyl)-2-Amino-1-Ethylphosphate (F19), PDB code: 2clo was solved by H.Ngo, N.Kimmich, R.Harris, D.Niks, L.Blumenstein, V.Kulik, T.R.Barends, I.Schlichting, M.F.Dunn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.93 / 1.5
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 182.730, 60.140, 67.510, 90.00, 94.61, 90.00
R / Rfree (%) 23.2 / 24.9

Sodium Binding Sites:

The binding sites of Sodium atom in the Tryptophan Synthase (External Aldimine State) in Complex with (Naphthalene-2'-Sulfonyl)-2-Amino-1-Ethylphosphate (F19) (pdb code 2clo). 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 (External Aldimine State) in Complex with (Naphthalene-2'-Sulfonyl)-2-Amino-1-Ethylphosphate (F19), PDB code: 2clo:

Sodium binding site 1 out of 1 in 2clo

Go back to Sodium Binding Sites List in 2clo
Sodium binding site 1 out of 1 in the Tryptophan Synthase (External Aldimine State) in Complex with (Naphthalene-2'-Sulfonyl)-2-Amino-1-Ethylphosphate (F19)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Tryptophan Synthase (External Aldimine State) in Complex with (Naphthalene-2'-Sulfonyl)-2-Amino-1-Ethylphosphate (F19) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1393

b:14.7
occ:1.00
 O B:SER308 2.4 10.5 1.0
O B:GLY232 2.4 14.0 1.0
O B:PHE306 2.5 18.9 1.0
O B:HOH2263 2.8 19.9 1.0
O B:HOH2301 2.9 26.9 1.0
C B:GLY232 3.5 12.2 1.0
C B:SER308 3.6 11.1 1.0
C B:PHE306 3.7 18.7 1.0
CG B:PRO270 3.8 9.0 1.0
CD B:PRO270 3.9 9.1 1.0
N B:SER308 4.0 15.7 1.0
O B:GLY268 4.0 11.6 1.0
CA B:GLY232 4.1 11.8 1.0
CB B:PHE306 4.2 18.8 1.0
O B:VAL231 4.3 10.6 1.0
CA B:PHE306 4.4 18.6 1.0
OG B:SER297 4.4 19.3 1.0
CA B:SER308 4.4 12.8 1.0
C B:PRO307 4.5 17.2 1.0
CD2 B:PHE306 4.6 18.4 1.0
N B:PHE306 4.6 18.0 1.0
N B:VAL309 4.6 10.5 1.0
CA B:VAL309 4.7 9.0 1.0
N B:PRO307 4.7 18.5 1.0
N B:GLY233 4.7 11.2 1.0
CB B:VAL309 4.7 10.0 1.0
CA B:PRO307 4.8 18.0 1.0
O B:LEU304 4.8 15.7 1.0
OE2 B:GLU256 4.8 12.6 1.0
CG B:PHE306 4.9 18.6 1.0
N B:GLY232 4.9 10.0 1.0
C B:VAL231 4.9 9.8 1.0
C B:GLY268 5.0 10.3 1.0

Reference:

H.Ngo, N.Kimmich, R.Harris, D.Niks, L.Blumenstein, V.Kulik, T.R.Barends, I.Schlichting, M.F.Dunn. Allosteric Regulation of Substrate Channeling in Tryptophan Synthase: Modulation of the L-Serine Reaction in Stage I of the Beta-Reaction By Alpha- Site Ligands. Biochemistry V. 46 7740 2007.
ISSN: ISSN 0006-2960
PubMed: 17559232
DOI: 10.1021/BI7003872
Page generated: Mon Oct 7 02:10:15 2024

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