Potassium in PDB 1bpj: Thymidylate Synthase R178T, R179T Double Mutant

All present enzymatic activity of Thymidylate Synthase R178T, R179T Double Mutant:
2.1.1.45;

The structure of Thymidylate Synthase R178T, R179T Double Mutant, PDB code: 1bpj was solved by R.J.Morse, J.S.Finer-Moore, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.40
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	78.800, 78.800, 243.800, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 28.1

The binding sites of Potassium atom in the Thymidylate Synthase R178T, R179T Double Mutant (pdb code 1bpj). 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 Thymidylate Synthase R178T, R179T Double Mutant, PDB code: 1bpj:

Potassium binding site 1 out of 1 in the Thymidylate Synthase R178T, R179T Double Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Thymidylate Synthase R178T, R179T Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K317 b:19.8 occ:0.50 O A:TRP185 2.4 7.1 1.0 OG A:SER183 2.9 3.3 1.0 C A:TRP185 3.6 7.2 1.0 CB A:SER183 3.8 2.0 1.0 CB A:TRP185 4.2 2.0 1.0 CH2 A:TRP153 4.3 19.8 1.0 CA A:TRP185 4.3 2.1 1.0 N A:TRP185 4.6 4.3 1.0 N A:ASN186 4.6 5.3 1.0 CD A:PRO187 4.8 2.0 1.0 CD1 A:TRP185 4.8 2.0 1.0 CA A:ASN186 4.8 6.3 1.0 CZ2 A:TRP153 4.9 23.0 1.0 CG A:TRP185 5.0 2.0 1.0

R.J.Morse, S.Kawase, D.V.Santi, J.Finer-Moore, R.M.Stroud. Energetic Contributions of Four Arginines to Phosphate-Binding in Thymidylate Synthase Are More Than Additive and Depend on Optimization of "Effective Charge Balance". Biochemistry V. 39 1011 2000.
ISSN: ISSN 0006-2960
PubMed: 10653645
DOI: 10.1021/BI9918590