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Potassium in PDB 6rtg: Crystal Structure of the Udp-Bound Glycosyltransferase Domain From the Ygt Toxin

Protein crystallography data

The structure of Crystal Structure of the Udp-Bound Glycosyltransferase Domain From the Ygt Toxin, PDB code: 6rtg was solved by C.Wirth, X.Bogdanovic, W.-C.Kao, C.Hunte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.56 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 164.270, 164.270, 47.740, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 22.3

Other elements in 6rtg:

The structure of Crystal Structure of the Udp-Bound Glycosyltransferase Domain From the Ygt Toxin also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Udp-Bound Glycosyltransferase Domain From the Ygt Toxin (pdb code 6rtg). 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 Crystal Structure of the Udp-Bound Glycosyltransferase Domain From the Ygt Toxin, PDB code: 6rtg:

Potassium binding site 1 out of 1 in 6rtg

Go back to Potassium Binding Sites List in 6rtg
Potassium binding site 1 out of 1 in the Crystal Structure of the Udp-Bound Glycosyltransferase Domain From the Ygt Toxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the Udp-Bound Glycosyltransferase Domain From the Ygt Toxin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:33.3
occ:1.00
OD1 A:ASP213 2.6 26.5 1.0
O A:PHE429 2.6 29.1 1.0
O A:GLU426 2.9 25.5 1.0
O A:HOH786 3.0 26.4 1.0
O A:HOH727 3.0 51.3 1.0
O1A A:UDP601 3.0 28.0 1.0
O A:HOH1055 3.0 46.0 1.0
O A:HOH909 3.3 41.9 1.0
CG A:ASP213 3.5 26.5 1.0
C A:PHE429 3.7 33.5 1.0
CB A:ASP213 3.7 26.7 1.0
MN A:MN602 3.7 26.0 1.0
O2A A:UDP601 3.7 36.7 1.0
C A:GLU426 3.9 29.9 1.0
PA A:UDP601 3.9 29.6 1.0
O A:HOH741 3.9 29.7 1.0
O A:HOH866 4.1 42.9 1.0
CA A:GLU427 4.3 25.8 1.0
O A:GLU427 4.5 28.5 1.0
N A:SER430 4.5 30.4 1.0
N A:GLU427 4.5 25.4 1.0
CA A:SER430 4.5 29.6 1.0
N A:PHE429 4.5 26.5 1.0
CA A:PHE429 4.6 31.1 1.0
C A:GLU427 4.6 33.1 1.0
OD2 A:ASP213 4.6 23.8 1.0
CB A:PHE429 4.8 25.4 1.0
CB A:GLU426 4.8 23.9 1.0
OE1 A:GLU426 4.8 34.5 1.0
OE1 A:GLU427 4.9 27.7 1.0
CA A:GLU426 4.9 22.7 1.0
O3B A:UDP601 4.9 25.8 1.0
N A:SER431 5.0 25.6 1.0
O5' A:UDP601 5.0 27.9 1.0

Reference:

G.S.Ost, C.Wirth, X.Bogdanovic, W.-C.Kao, B.Schorch, P.J.K.Aktories, M.Westphal, P.Papatheodorou, C.Schwan, A.Schlosser, W.Driever, T.Jank, C.Hunte, K.Aktories. Inverse Control of Rab Proteins By Yersinia Adp-Ribosyltransferase and Glycosyltransferase Related to Clostridial Glucosylating Toxins Sci Adv 2020.
ISSN: ESSN 2375-2548
DOI: 10.1126/SCIADV.AAZ2094
Page generated: Mon Aug 12 17:30:15 2024

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