|
Atomistry » Potassium » PDB 1a3w-1d7u » 1bpj | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 1a3w-1d7u » 1bpj » |
Potassium in PDB 1bpj: Thymidylate Synthase R178T, R179T Double MutantEnzymatic activity of Thymidylate Synthase R178T, R179T Double Mutant
All present enzymatic activity of Thymidylate Synthase R178T, R179T Double Mutant:
2.1.1.45; Protein crystallography data
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:
Potassium Binding Sites:
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 1bpjGo back to![]() ![]()
Potassium binding site 1 out
of 1 in the Thymidylate Synthase R178T, R179T Double Mutant
![]() Mono view ![]() Stereo pair view
Reference:
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.
Page generated: Mon Aug 12 04:04:48 2024
ISSN: ISSN 0006-2960 PubMed: 10653645 DOI: 10.1021/BI9918590 |
Last articlesBr in 2XNTBr in 2X3H Br in 2XO8 Br in 2XMD Br in 2XC6 Br in 2X6E Br in 2XAF Br in 2XAG Br in 2X42 Br in 2X6D |
© Copyright 2008-2020 by atomistry.com | ||
Home | Site Map | Copyright | Contact us | Privacy |