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Potassium in PDB 4zag: Structure of Ubix E49Q Mutant in Complex with Oxidised Fmn and Dimethylallyl Monophosphate

Protein crystallography data

The structure of Structure of Ubix E49Q Mutant in Complex with Oxidised Fmn and Dimethylallyl Monophosphate, PDB code: 4zag was solved by M.D.White, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.65 / 1.68
Space group F 2 3
Cell size a, b, c (Å), α, β, γ (°) 142.310, 142.310, 142.310, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 18

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Ubix E49Q Mutant in Complex with Oxidised Fmn and Dimethylallyl Monophosphate (pdb code 4zag). 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 Ubix E49Q Mutant in Complex with Oxidised Fmn and Dimethylallyl Monophosphate, PDB code: 4zag:

Potassium binding site 1 out of 1 in 4zag

Go back to Potassium Binding Sites List in 4zag
Potassium binding site 1 out of 1 in the Structure of Ubix E49Q Mutant in Complex with Oxidised Fmn and Dimethylallyl Monophosphate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Ubix E49Q Mutant in Complex with Oxidised Fmn and Dimethylallyl Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K304

b:34.4
occ:1.00
O A:HOH507 2.9 25.9 1.0
OG A:SER15 2.9 26.1 1.0
CB A:GLN49 3.4 36.0 1.0
CG A:GLN49 3.4 37.4 1.0
CB A:SER15 3.8 23.4 1.0
CA A:SER15 3.9 20.8 1.0
CG1 A:VAL45 3.9 22.7 1.0
CD A:GLN49 4.3 37.6 1.0
N A:GLY16 4.4 21.1 1.0
NE2 A:GLN49 4.5 32.4 1.0
C A:SER15 4.7 22.6 1.0
O A:VAL45 5.0 24.4 1.0
CA A:GLN49 5.0 32.1 1.0

Reference:

M.D.White, K.A.Payne, K.Fisher, S.A.Marshall, D.Parker, N.J.Rattray, D.K.Trivedi, R.Goodacre, S.E.Rigby, N.S.Scrutton, S.Hay, D.Leys. Ubix Is A Flavin Prenyltransferase Required For Bacterial Ubiquinone Biosynthesis. Nature V. 522 497 2015.
ISSN: ESSN 1476-4687
PubMed: 26083743
DOI: 10.1038/NATURE14559
Page generated: Sun Dec 13 23:53:11 2020

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