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Potassium in PDB 5npr: The Human O-Glcnac Transferase in Complex with A Thiol-Linked Bisubstrate Inhibitor

Enzymatic activity of The Human O-Glcnac Transferase in Complex with A Thiol-Linked Bisubstrate Inhibitor

All present enzymatic activity of The Human O-Glcnac Transferase in Complex with A Thiol-Linked Bisubstrate Inhibitor:
2.4.1.255;

Protein crystallography data

The structure of The Human O-Glcnac Transferase in Complex with A Thiol-Linked Bisubstrate Inhibitor, PDB code: 5npr was solved by K.Rafie, D.M.F.Van Aalten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.01 / 1.85
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 138.038, 150.951, 200.540, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 23.6

Potassium Binding Sites:

The binding sites of Potassium atom in the The Human O-Glcnac Transferase in Complex with A Thiol-Linked Bisubstrate Inhibitor (pdb code 5npr). 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 The Human O-Glcnac Transferase in Complex with A Thiol-Linked Bisubstrate Inhibitor, PDB code: 5npr:

Potassium binding site 1 out of 1 in 5npr

Go back to Potassium Binding Sites List in 5npr
Potassium binding site 1 out of 1 in the The Human O-Glcnac Transferase in Complex with A Thiol-Linked Bisubstrate Inhibitor


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Human O-Glcnac Transferase in Complex with A Thiol-Linked Bisubstrate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1101

b:70.3
occ:1.00
O A:HOH1556 2.5 44.9 1.0
O A:HOH1325 2.6 31.1 0.5
O A:HOH1513 2.7 46.5 1.0
O A:HOH1203 4.1 39.8 1.0
O A:HOH1527 4.3 45.4 1.0
O A:HOH1554 4.4 50.6 1.0
OE2 A:GLU437 4.5 41.5 1.0
O A:HOH1537 4.7 35.6 1.0

Reference:

K.Rafie, A.Gorelik, R.Trapannone, V.S.Borodkin, D.M.F.Van Aalten. Thio-Linked Udp-Peptide Conjugates As O-Glcnac Transferase Inhibitors. Bioconjug. Chem. V. 29 1834 2018.
ISSN: ISSN 1520-4812
PubMed: 29723473
DOI: 10.1021/ACS.BIOCONJCHEM.8B00194
Page generated: Sat Aug 9 09:35:47 2025

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