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Potassium in PDB 5fg1: Structure of the Conserved Yeast Listerin (LTN1) Selenomethionine- Substituted N-Terminal Domain, Trigonal Form

Protein crystallography data

The structure of Structure of the Conserved Yeast Listerin (LTN1) Selenomethionine- Substituted N-Terminal Domain, Trigonal Form, PDB code: 5fg1 was solved by S.K.Doamekpor, C.D.Lima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.79 / 2.55
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 58.088, 58.088, 347.131, 90.00, 90.00, 120.00
R / Rfree (%) 20.1 / 24.3

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of the Conserved Yeast Listerin (LTN1) Selenomethionine- Substituted N-Terminal Domain, Trigonal Form (pdb code 5fg1). 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 the Conserved Yeast Listerin (LTN1) Selenomethionine- Substituted N-Terminal Domain, Trigonal Form, PDB code: 5fg1:

Potassium binding site 1 out of 1 in 5fg1

Go back to Potassium Binding Sites List in 5fg1
Potassium binding site 1 out of 1 in the Structure of the Conserved Yeast Listerin (LTN1) Selenomethionine- Substituted N-Terminal Domain, Trigonal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of the Conserved Yeast Listerin (LTN1) Selenomethionine- Substituted N-Terminal Domain, Trigonal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K501

b:75.7
occ:1.00
OG A:SER245 2.7 67.7 1.0
O A:GLU188 2.7 62.0 1.0
OH A:TYR208 2.8 60.2 1.0
O A:VAL185 2.8 53.1 1.0
HH A:TYR208 2.9 72.3 1.0
HG A:SER245 3.1 81.3 1.0
HA A:ASN189 3.4 64.8 1.0
HB3 A:ASN189 3.5 68.8 1.0
CZ A:TYR208 3.7 59.1 1.0
HB3 A:SER245 3.7 78.9 1.0
CB A:SER245 3.7 65.7 1.0
C A:GLU188 3.9 61.2 1.0
C A:VAL185 3.9 51.5 1.0
HB2 A:SER245 4.0 78.9 1.0
HE2 A:TYR208 4.0 69.8 1.0
CA A:ASN189 4.1 54.0 1.0
CB A:ASN189 4.1 57.4 1.0
CE2 A:TYR208 4.2 58.1 1.0
HA A:VAL185 4.2 59.9 1.0
O A:ILE184 4.3 54.5 1.0
HB2 A:ASN189 4.3 68.8 1.0
OD2 A:ASP243 4.4 72.5 1.0
N A:ASN189 4.5 53.2 1.0
HA A:VAL186 4.5 71.5 1.0
CE1 A:TYR208 4.5 57.6 1.0
HE1 A:TYR208 4.6 69.1 1.0
CA A:VAL185 4.7 49.9 1.0
O A:VAL186 4.7 59.0 1.0
H A:GLU188 4.7 75.2 1.0
N A:VAL186 4.8 58.3 1.0
HD12 A:ILE212 4.8 70.0 1.0
C A:VAL186 4.9 58.4 1.0
CA A:VAL186 5.0 59.6 1.0
OD1 A:ASP243 5.0 72.3 1.0
HA A:SER245 5.0 79.4 1.0
CG A:ASP243 5.0 72.8 1.0
CA A:SER245 5.0 66.2 1.0

Reference:

S.K.Doamekpor, J.W.Lee, N.L.Hepowit, C.Wu, C.Charenton, M.Leonard, M.H.Bengtson, K.R.Rajashankar, M.S.Sachs, C.D.Lima, C.A.Joazeiro. Structure and Function of the Yeast Listerin (LTN1) Conserved N-Terminal Domain in Binding to Stalled 60S Ribosomal Subunits. Proc.Natl.Acad.Sci.Usa V. 113 E4151 2016.
ISSN: ESSN 1091-6490
PubMed: 27385828
DOI: 10.1073/PNAS.1605951113
Page generated: Mon Aug 12 13:31:28 2024

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