Calcium in PDB 7zxw: Catalytic Domain of Udp-Glucose Glycoprotein Glucosyltransferase From Chaetomium Thermophilum in Complex with the 5-[(Morpholin-4-Yl) Methyl]Quinolin-8-Ol Inhibitor

The structure of Catalytic Domain of Udp-Glucose Glycoprotein Glucosyltransferase From Chaetomium Thermophilum in Complex with the 5-[(Morpholin-4-Yl) Methyl]Quinolin-8-Ol Inhibitor, PDB code: 7zxw was solved by J.D.Le Cornu, R.Ibba, P.Roversi, N.Zitzmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.01 / 2.25
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	118.009, 118.009, 68.373, 90, 90, 120
R / Rfree (%)	20.3 / 24.1

The binding sites of Calcium atom in the Catalytic Domain of Udp-Glucose Glycoprotein Glucosyltransferase From Chaetomium Thermophilum in Complex with the 5-[(Morpholin-4-Yl) Methyl]Quinolin-8-Ol Inhibitor (pdb code 7zxw). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Catalytic Domain of Udp-Glucose Glycoprotein Glucosyltransferase From Chaetomium Thermophilum in Complex with the 5-[(Morpholin-4-Yl) Methyl]Quinolin-8-Ol Inhibitor, PDB code: 7zxw:

Calcium binding site 1 out of 1 in the Catalytic Domain of Udp-Glucose Glycoprotein Glucosyltransferase From Chaetomium Thermophilum in Complex with the 5-[(Morpholin-4-Yl) Methyl]Quinolin-8-Ol Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Catalytic Domain of Udp-Glucose Glycoprotein Glucosyltransferase From Chaetomium Thermophilum in Complex with the 5-[(Morpholin-4-Yl) Methyl]Quinolin-8-Ol Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1501 b:27.5 occ:1.00 O A:HOH1604 2.3 25.4 1.0 O2' A:UPG1502 2.3 33.7 1.0 OD2 A:ASP1304 2.3 32.0 1.0 OD2 A:ASP1302 2.4 29.3 1.0 OD1 A:ASP1304 2.4 29.1 1.0 O2B A:UPG1502 2.5 31.4 1.0 OD1 A:ASP1435 2.5 25.2 1.0 CG A:ASP1304 2.7 28.7 1.0 CG A:ASP1302 3.4 28.2 1.0 CG A:ASP1435 3.5 25.1 1.0 C2' A:UPG1502 3.6 33.7 1.0 PB A:UPG1502 3.6 33.0 1.0 OD2 A:ASP1435 3.7 26.1 1.0 O3B A:UPG1502 3.7 33.2 1.0 C3' A:UPG1502 3.9 33.3 1.0 CB A:ASP1302 4.1 23.9 1.0 O3' A:UPG1502 4.1 32.9 1.0 NZ A:LYS1446 4.1 39.0 1.0 CB A:ASP1304 4.1 24.9 1.0 C1' A:UPG1502 4.2 33.6 1.0 OD1 A:ASP1302 4.2 30.5 1.0 O2A A:UPG1502 4.3 36.8 1.0 O A:HOH1685 4.3 28.9 1.0 O3A A:UPG1502 4.6 35.5 1.0 N A:LEU1436 4.6 24.7 1.0 PA A:UPG1502 4.7 37.0 1.0 O1A A:UPG1502 4.7 36.8 1.0 C A:LEU1436 4.7 27.2 1.0 O1B A:UPG1502 4.7 33.2 1.0 O A:LEU1436 4.7 28.6 1.0 N A:CYS1437 4.8 27.0 1.0 CA A:CYS1437 4.8 27.5 1.0 CB A:ASP1435 4.8 22.6 1.0

A.T.Caputo, R.Ibba, J.D.Le Cornu, B.Darlot, M.Hensen, C.B.Lipp, G.Marciano, S.Vasiljevic, N.Zitzmann, P.Roversi. Crystal Polymorphism in Fragment-Based Lead Discovery of Ligands of the Catalytic Domain of Uggt, the Glycoprotein Folding Quality Control Checkpoint. Front Mol Biosci 2022.
ISSN: ESSN 2296-889X
DOI: 10.3389/FMOLB.2022.960248