Atomistry » Potassium » PDB 1a3w-1d7u » 1beu
Atomistry »
  Potassium »
    PDB 1a3w-1d7u »
      1beu »

Potassium in PDB 1beu: Trp Synthase (D60N-Ipp-Ser) with K+

Enzymatic activity of Trp Synthase (D60N-Ipp-Ser) with K+

All present enzymatic activity of Trp Synthase (D60N-Ipp-Ser) with K+:
4.2.1.20;

Protein crystallography data

The structure of Trp Synthase (D60N-Ipp-Ser) with K+, PDB code: 1beu was solved by S.Rhee, A.Mozzarelli, 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 (°) 182.300, 59.700, 67.400, 90.00, 94.60, 90.00
R / Rfree (%) 21.9 / 27.8

Potassium Binding Sites:

The binding sites of Potassium atom in the Trp Synthase (D60N-Ipp-Ser) with K+ (pdb code 1beu). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Trp Synthase (D60N-Ipp-Ser) with K+, PDB code: 1beu:

Potassium binding site 1 out of 1 in 1beu

Go back to Potassium Binding Sites List in 1beu
Potassium binding site 1 out of 1 in the Trp Synthase (D60N-Ipp-Ser) with K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Trp Synthase (D60N-Ipp-Ser) with K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K400

b:31.2
occ:1.00
O B:PHE306 2.5 32.2 1.0
O B:GLY232 2.6 17.0 1.0
O B:HOH454 2.6 23.3 1.0
O B:SER308 2.8 19.5 1.0
C B:GLY232 3.6 15.0 1.0
O B:GLY268 3.6 14.3 1.0
C B:PHE306 3.7 28.5 1.0
CD B:PRO270 3.9 16.0 1.0
CG1 B:VAL309 3.9 21.9 1.0
C B:SER308 3.9 16.3 1.0
CG B:PRO270 3.9 13.2 1.0
CA B:GLY232 4.0 12.6 1.0
CB B:PHE306 4.1 28.3 1.0
O B:VAL231 4.2 12.4 1.0
CA B:PHE306 4.3 28.9 1.0
N B:SER308 4.3 17.6 1.0
N B:PHE306 4.4 31.9 1.0
OG B:SER297 4.4 38.5 1.0
CD2 B:PHE306 4.5 27.9 1.0
O B:LEU304 4.5 27.2 1.0
C B:GLY268 4.7 10.9 1.0
CG B:PHE306 4.7 29.0 1.0
N B:GLY233 4.7 15.3 1.0
CA B:SER308 4.7 16.7 1.0
N B:PRO307 4.7 29.0 1.0
C B:PRO307 4.8 21.1 1.0
N B:VAL309 4.9 13.9 1.0
OE2 B:GLU256 4.9 18.4 1.0
C B:VAL231 4.9 13.1 1.0
N B:GLY232 4.9 13.6 1.0
O B:HOH457 4.9 18.4 1.0
CA B:VAL309 5.0 11.5 1.0
CA B:PRO307 5.0 24.8 1.0

Reference:

S.Rhee, E.W.Miles, A.Mozzarelli, D.R.Davies. Cryocrystallography and Microspectrophotometry of A Mutant (Alpha D60N) Tryptophan Synthase Alpha 2 Beta 2 Complex Reveals Allosteric Roles of Alpha ASP60. Biochemistry V. 37 10653 1998.
ISSN: ISSN 0006-2960
PubMed: 9692955
DOI: 10.1021/BI980779D
Page generated: Sun Dec 13 22:41:42 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy