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Sodium in PDB 1ubs: Tryptophan Synthase (E.C.4.2.1.20) with A Mutation of Lys 87->Thr in the B Subunit and in the Presence of Ligand L-Serine

Enzymatic activity of Tryptophan Synthase (E.C.4.2.1.20) with A Mutation of Lys 87->Thr in the B Subunit and in the Presence of Ligand L-Serine

All present enzymatic activity of Tryptophan Synthase (E.C.4.2.1.20) with A Mutation of Lys 87->Thr in the B Subunit and in the Presence of Ligand L-Serine:
4.2.1.20;

Protein crystallography data

The structure of Tryptophan Synthase (E.C.4.2.1.20) with A Mutation of Lys 87->Thr in the B Subunit and in the Presence of Ligand L-Serine, PDB code: 1ubs was solved by S.Rhee, K.Parris, S.A.Ahmed, E.W.Miles, D.R.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 184.200, 61.800, 67.800, 90.00, 94.80, 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) with A Mutation of Lys 87->Thr in the B Subunit and in the Presence of Ligand L-Serine (pdb code 1ubs). 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) with A Mutation of Lys 87->Thr in the B Subunit and in the Presence of Ligand L-Serine, PDB code: 1ubs:

Sodium binding site 1 out of 1 in 1ubs

Go back to Sodium Binding Sites List in 1ubs
Sodium binding site 1 out of 1 in the Tryptophan Synthase (E.C.4.2.1.20) with A Mutation of Lys 87->Thr in the B Subunit and in the Presence of Ligand L-Serine


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) with A Mutation of Lys 87->Thr in the B Subunit and in the Presence of Ligand L-Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na400

b:21.7
occ:1.00
 O B:GLY232 2.1 20.2 1.0
O B:HOH432 2.2 28.0 1.0
O B:HOH412 2.4 17.6 1.0
O B:PHE306 2.4 25.0 1.0
O B:SER308 2.4 20.8 1.0
C B:GLY232 3.3 16.6 1.0
C B:PHE306 3.6 23.2 1.0
C B:SER308 3.6 17.1 1.0
CA B:GLY232 3.9 15.4 1.0
CG B:PRO270 4.0 20.5 1.0
N B:SER308 4.1 17.1 1.0
CD B:PRO270 4.1 21.6 1.0
O B:GLY268 4.3 19.3 1.0
OG B:SER297 4.3 33.3 1.0
CA B:PHE306 4.3 21.2 1.0
CB B:PHE306 4.3 17.0 1.0
N B:GLY233 4.4 16.3 1.0
N B:VAL309 4.4 15.9 1.0
O B:VAL231 4.4 21.6 1.0
CA B:SER308 4.5 17.4 1.0
CA B:VAL309 4.5 15.9 1.0
N B:PHE306 4.5 16.9 1.0
N B:PRO307 4.6 26.4 1.0
CD2 B:PHE306 4.6 21.8 1.0
CB B:VAL309 4.6 24.9 1.0
C B:PRO307 4.7 21.0 1.0
CA B:GLY233 4.7 12.2 1.0
N B:GLY232 4.8 12.3 1.0
O B:LEU304 4.8 23.6 1.0
CA B:PRO307 4.8 22.8 1.0
OE1 B:GLU256 4.9 24.7 1.0
C B:VAL231 4.9 15.8 1.0
CG B:PHE306 4.9 19.2 1.0

Reference:

S.Rhee, K.D.Parris, C.C.Hyde, S.A.Ahmed, E.W.Miles, D.R.Davies. Crystal Structures of A Mutant (BETAK87T) Tryptophan Synthase ALPHA2BETA2 Complex with Ligands Bound to the Active Sites of the Alpha- and Beta-Subunits Reveal Ligand-Induced Conformational Changes. Biochemistry V. 36 7664 1997.
ISSN: ISSN 0006-2960
PubMed: 9201907
DOI: 10.1021/BI9700429
Page generated: Sun Oct 6 22:45:04 2024

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