Potassium in PDB 5txr: Structure of Alas From S. Cerevisiae Non-Covalently Bound to Plp Cofactor

All present enzymatic activity of Structure of Alas From S. Cerevisiae Non-Covalently Bound to Plp Cofactor:
2.3.1.37;

The structure of Structure of Alas From S. Cerevisiae Non-Covalently Bound to Plp Cofactor, PDB code: 5txr was solved by B.L.Brown, R.A.Grant, J.R.Kardon, R.T.Sauer, T.A.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.73 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.613, 64.878, 95.693, 90.00, 95.86, 90.00
R / Rfree (%)	14.2 / 17.2

The binding sites of Potassium atom in the Structure of Alas From S. Cerevisiae Non-Covalently Bound to Plp Cofactor (pdb code 5txr). 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 Structure of Alas From S. Cerevisiae Non-Covalently Bound to Plp Cofactor, PDB code: 5txr:

Potassium binding site 1 out of 1 in the Structure of Alas From S. Cerevisiae Non-Covalently Bound to Plp Cofactor


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Alas From S. Cerevisiae Non-Covalently Bound to Plp Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:K602 b:20.0 occ:1.00 OG A:SER304 2.7 14.4 1.0 O A:HOH1044 2.7 48.6 1.0 OG1 A:THR315 2.9 14.9 1.0 O A:ASN316 2.9 13.9 1.0 O A:THR315 3.0 12.6 1.0 O A:HOH1066 3.0 23.9 1.0 O A:HOH1010 3.0 47.6 1.0 HG A:SER304 3.2 14.4 1.0 HG1 A:THR315 3.2 14.9 1.0 C A:THR315 3.5 13.2 1.0 C A:ASN316 3.6 13.5 1.0 HB3 A:SER304 3.6 14.8 1.0 O A:HOH1065 3.7 48.8 1.0 CB A:SER304 3.7 14.8 1.0 HA A:ASP317 3.9 16.4 1.0 HA A:SER304 3.9 9.5 1.0 CB A:THR315 4.0 15.6 1.0 H A:THR315 4.0 14.5 1.0 N A:ASN316 4.0 12.7 1.0 HA A:ASN316 4.2 11.3 1.0 CA A:ASN316 4.2 11.3 1.0 CA A:THR315 4.2 12.4 1.0 HB A:THR315 4.3 15.6 1.0 O A:HOH1034 4.3 30.0 1.0 O A:HOH959 4.3 33.5 1.0 N A:ASP317 4.3 17.9 1.0 CA A:SER304 4.4 9.5 1.0 H A:GLY319 4.5 15.4 1.0 HB2 A:PRO313 4.5 16.3 1.0 HB2 A:SER304 4.5 14.8 1.0 CA A:ASP317 4.5 16.4 1.0 HA2 A:GLY319 4.5 18.2 1.0 N A:THR315 4.6 14.5 1.0 H A:ASN316 4.6 12.7 1.0

B.L.Brown, J.R.Kardon, R.T.Sauer, T.A.Baker. Structure of the Mitochondrial Aminolevulinic Acid Synthase, A Key Heme Biosynthetic Enzyme. Structure V. 26 580 2018.
ISSN: ISSN 1878-4186
PubMed: 29551290
DOI: 10.1016/J.STR.2018.02.012