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Potassium in PDB 1bp0: Thymidylate Synthase R23I Mutant

Enzymatic activity of Thymidylate Synthase R23I Mutant

All present enzymatic activity of Thymidylate Synthase R23I Mutant:
2.1.1.45;

Protein crystallography data

The structure of Thymidylate Synthase R23I Mutant, PDB code: 1bp0 was solved by R.Morse, J.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 (°) 79.100, 79.100, 243.300, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 27.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Thymidylate Synthase R23I Mutant (pdb code 1bp0). 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 R23I Mutant, PDB code: 1bp0:

Potassium binding site 1 out of 1 in 1bp0

Go back to Potassium Binding Sites List in 1bp0
Potassium binding site 1 out of 1 in the Thymidylate Synthase R23I 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 R23I Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K318

b:33.5
occ:0.50
O A:TRP185 2.4 10.7 1.0
OG A:SER183 2.8 12.0 1.0
C A:TRP185 3.6 12.8 1.0
CB A:SER183 3.7 15.1 1.0
CH2 A:TRP153 4.2 19.0 1.0
CB A:TRP185 4.3 9.4 1.0
CA A:TRP185 4.3 9.8 1.0
N A:TRP185 4.6 8.8 1.0
CD A:PRO187 4.6 9.5 1.0
N A:ASN186 4.7 15.7 1.0
CZ2 A:TRP153 4.8 20.6 1.0
CD1 A:TRP185 4.8 4.0 1.0
CA A:ASN186 4.9 15.3 1.0

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.
ISSN: ISSN 0006-2960
PubMed: 10653645
DOI: 10.1021/BI9918590
Page generated: Mon Aug 12 04:04:22 2024

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