Calcium in PDB 5ub5: Human POGLUT1 in Complex with Human NOTCH1 EGF12 S458T Mutant and Udp

All present enzymatic activity of Human POGLUT1 in Complex with Human NOTCH1 EGF12 S458T Mutant and Udp:
2.4.2.26;

The structure of Human POGLUT1 in Complex with Human NOTCH1 EGF12 S458T Mutant and Udp, PDB code: 5ub5 was solved by Z.Li, J.M.Rini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.90 / 2.09
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.951, 74.072, 83.583, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 19.3

The binding sites of Calcium atom in the Human POGLUT1 in Complex with Human NOTCH1 EGF12 S458T Mutant and Udp (pdb code 5ub5). 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 Human POGLUT1 in Complex with Human NOTCH1 EGF12 S458T Mutant and Udp, PDB code: 5ub5:

Calcium binding site 1 out of 1 in the Human POGLUT1 in Complex with Human NOTCH1 EGF12 S458T Mutant and Udp


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Human POGLUT1 in Complex with Human NOTCH1 EGF12 S458T Mutant and Udp within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1001 b:39.8 occ:1.00 O B:HOH1103 2.2 38.5 1.0 OD1 B:ASP469 2.3 32.6 1.0 OE1 B:GLU455 2.5 41.5 1.0 O B:GLN470 2.5 41.7 1.0 O B:VAL453 2.5 43.9 1.0 OD2 B:ASP452 2.6 50.6 1.0 O B:GLU473 2.9 37.4 1.0 OD1 B:ASP452 3.2 51.6 1.0 H B:GLU473 3.2 53.8 1.0 CG B:ASP452 3.2 52.1 1.0 HA B:ASN454 3.5 39.1 1.0 CD B:GLU455 3.5 39.9 1.0 CG B:ASP469 3.5 33.2 1.0 H B:GLU455 3.5 35.5 1.0 H B:GLY472 3.5 67.8 1.0 C B:GLN470 3.7 42.8 1.0 H B:GLN470 3.7 43.9 1.0 HA2 B:GLY472 3.7 68.3 1.0 OE2 B:GLU455 3.7 42.0 1.0 C B:VAL453 3.7 42.2 1.0 N B:GLU473 3.7 44.8 1.0 N B:GLY472 3.9 56.5 1.0 C B:GLU473 3.9 35.8 1.0 N B:GLN470 4.0 36.5 1.0 OD2 B:ASP469 4.1 32.6 1.0 CA B:GLY472 4.1 56.9 1.0 HA B:ASP469 4.3 41.6 1.0 N B:GLU455 4.3 29.5 1.0 CA B:ASN454 4.3 32.6 1.0 C B:GLY472 4.3 53.9 1.0 CA B:GLN470 4.4 40.7 1.0 N B:ASN454 4.5 36.9 1.0 CA B:GLU473 4.5 39.9 1.0 H B:VAL453 4.5 59.0 1.0 C B:ASP469 4.5 37.9 1.0 N B:VAL453 4.5 49.1 1.0 CB B:ASP469 4.6 34.3 1.0 HA B:ILE471 4.6 63.9 1.0 HB3 B:PHE474 4.7 36.3 1.0 CA B:ASP469 4.7 34.6 1.0 CB B:ASP452 4.7 55.3 1.0 HB2 B:GLU455 4.7 36.0 1.0 C B:ILE471 4.7 54.3 1.0 CA B:VAL453 4.7 48.0 1.0 N B:ILE471 4.7 47.5 1.0 HA B:GLU473 4.7 47.9 1.0 HB B:VAL453 4.8 67.9 1.0 C B:ASN454 4.8 29.2 1.0 CG B:GLU455 4.8 34.5 1.0 HB2 B:ASP469 4.9 41.2 1.0 C B:ASP452 4.9 54.0 1.0 HA B:PHE474 4.9 38.4 1.0 N B:PHE474 4.9 34.0 1.0 HB3 B:ASP452 5.0 66.4 1.0

Z.Li, M.Fischer, M.Satkunarajah, D.Zhou, S.G.Withers, J.M.Rini. Structural Basis of Notch O-Glucosylation and O-Xylosylation By Mammalian Protein-O-Glucosyltransferase 1 (POGLUT1). Nat Commun V. 8 185 2017.
ISSN: ESSN 2041-1723
PubMed: 28775322
DOI: 10.1038/S41467-017-00255-7