Atomistry » Sodium » PDB 1w5n-1x7d » 1wbj
Atomistry »
  Sodium »
    PDB 1w5n-1x7d »
      1wbj »

Sodium in PDB 1wbj: Wildtype Tryptophan Synthase Complexed with Glycerol Phosphate

Enzymatic activity of Wildtype Tryptophan Synthase Complexed with Glycerol Phosphate

All present enzymatic activity of Wildtype Tryptophan Synthase Complexed with Glycerol Phosphate:
4.2.1.20;

Protein crystallography data

The structure of Wildtype Tryptophan Synthase Complexed with Glycerol Phosphate, PDB code: 1wbj was solved by V.Kulik, M.Weyand, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 182.045, 59.558, 67.409, 90.00, 94.56, 90.00
R / Rfree (%) 17.9 / 20.2

Sodium Binding Sites:

The binding sites of Sodium atom in the Wildtype Tryptophan Synthase Complexed with Glycerol Phosphate (pdb code 1wbj). 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 Wildtype Tryptophan Synthase Complexed with Glycerol Phosphate, PDB code: 1wbj:

Sodium binding site 1 out of 1 in 1wbj

Go back to Sodium Binding Sites List in 1wbj
Sodium binding site 1 out of 1 in the Wildtype Tryptophan Synthase Complexed with Glycerol Phosphate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Wildtype Tryptophan Synthase Complexed with Glycerol Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1393

b:10.3
occ:1.00
O B:GLY232 2.3 10.7 1.0
O B:SER308 2.4 9.9 1.0
O B:HOH2237 2.4 11.5 1.0
O B:HOH2243 2.4 14.0 1.0
O B:PHE306 2.4 14.4 1.0
C B:GLY232 3.4 9.2 1.0
C B:SER308 3.5 9.9 1.0
C B:PHE306 3.6 12.3 1.0
CG B:PRO270 3.8 10.0 1.0
CD B:PRO270 3.9 9.9 1.0
N B:SER308 3.9 11.7 1.0
O B:GLY268 4.1 11.8 1.0
CA B:GLY232 4.1 9.5 1.0
CB B:PHE306 4.3 11.5 1.0
CA B:SER308 4.3 10.4 1.0
OG B:SER297 4.4 17.8 1.0
CA B:PHE306 4.4 12.7 1.0
CD2 B:PHE306 4.4 14.6 1.0
C B:PRO307 4.4 13.3 1.0
O B:VAL231 4.5 9.4 1.0
N B:GLY233 4.5 8.9 1.0
N B:VAL309 4.5 9.8 1.0
N B:PRO307 4.6 11.7 1.0
CA B:VAL309 4.6 8.1 1.0
N B:PHE306 4.6 12.8 1.0
O B:LEU304 4.6 14.6 1.0
CB B:VAL309 4.6 9.6 1.0
CA B:PRO307 4.6 11.5 1.0
CA B:GLY233 4.8 7.9 1.0
OE2 B:GLU256 4.8 11.2 1.0
CG B:PHE306 4.8 12.4 1.0
N B:GLY232 5.0 7.7 1.0

Reference:

V.Kulik, E.Hartmann, M.Weyand, M.Frey, A.Gierl, D.Niks, M.F.Dunn, I.Schlichting. On the Structural Basis of the Catalytic Mechanism and the Regulation of the Alpha Subunit of Tryptophan Synthase From Salmonella Typhimurium and BX1 From Maize, Two Evolutionarily Related Enzymes. J.Mol.Biol. V. 352 608 2005.
ISSN: ISSN 0022-2836
PubMed: 16120446
DOI: 10.1016/J.JMB.2005.07.014
Page generated: Tue Dec 15 05:41:09 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy