Chlorine in PDB 5l0t: Human POGLUT1 in Complex with Egf(+) and Udp

All present enzymatic activity of Human POGLUT1 in Complex with Egf(+) and Udp:
2.4.2.26;

The structure of Human POGLUT1 in Complex with Egf(+) and Udp, PDB code: 5l0t 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)	43.98 / 1.43
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.660, 75.200, 82.950, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 17.3

The structure of Human POGLUT1 in Complex with Egf(+) and Udp also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Chlorine atom in the Human POGLUT1 in Complex with Egf(+) and Udp (pdb code 5l0t). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Human POGLUT1 in Complex with Egf(+) and Udp, PDB code: 5l0t:

Chlorine binding site 1 out of 1 in the Human POGLUT1 in Complex with Egf(+) and Udp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human POGLUT1 in Complex with Egf(+) and Udp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl407 b:25.7 occ:1.00 H A:SER106 2.4 26.0 1.0 HB2 A:SER106 2.8 29.8 1.0 HA A:PHE104 3.0 34.2 1.0 O A:HOH651 3.1 21.1 1.0 HD2 A:PRO105 3.1 29.8 1.0 HB3 A:PHE104 3.2 32.5 1.0 N A:SER106 3.2 21.6 1.0 HD1 A:PHE104 3.2 35.5 1.0 O B:HOH219 3.3 24.1 1.0 H A:ARG107 3.3 23.4 1.0 C A:PHE104 3.3 27.9 1.0 N A:PRO105 3.4 23.8 1.0 HG3 A:ARG107 3.4 23.8 1.0 CA A:PHE104 3.5 28.5 1.0 CB A:SER106 3.6 24.9 1.0 HD21 B:ASN35 3.7 34.0 1.0 CD A:PRO105 3.7 24.8 1.0 CB A:PHE104 3.8 27.1 1.0 O A:PHE104 3.8 26.2 1.0 ND2 B:ASN35 3.8 28.4 1.0 CA A:SER106 3.9 21.6 1.0 N A:ARG107 4.0 19.5 1.0 OG A:SER106 4.0 31.8 1.0 CD1 A:PHE104 4.1 29.6 1.0 HD22 B:ASN35 4.1 34.0 1.0 HH B:TYR23 4.1 31.2 1.0 C A:PRO105 4.2 28.2 1.0 HD3 A:PRO105 4.2 29.8 1.0 CG B:ASN35 4.2 26.6 1.0 HG A:SER106 4.2 38.2 1.0 OH B:TYR23 4.3 26.0 1.0 CA A:PRO105 4.3 27.3 1.0 HB3 A:SER106 4.4 29.8 1.0 C A:SER106 4.4 21.5 1.0 CG A:ARG107 4.4 19.8 1.0 CG A:PHE104 4.4 28.1 1.0 HE A:ARG107 4.5 23.5 1.0 OD1 B:ASN35 4.5 33.0 1.0 HB2 B:PRO9 4.5 26.2 1.0 HB2 A:PHE104 4.6 32.5 1.0 O B:PRO9 4.7 21.7 1.0 HB2 A:PRO105 4.7 31.2 1.0 HA B:PRO9 4.7 25.6 1.0 HA A:SER106 4.7 25.9 1.0 HB3 B:PRO9 4.8 26.2 1.0 HG2 A:ARG107 4.8 23.8 1.0 HE21 B:GLN11 4.9 30.4 1.0 N A:PHE104 4.9 29.1 1.0 CG A:PRO105 4.9 34.7 1.0 HA2 A:GLY169 4.9 24.0 1.0 HB3 B:ASN35 4.9 30.2 1.0 O A:HOH816 4.9 29.0 1.0 CB A:PRO105 4.9 26.0 1.0 HB2 A:ARG107 4.9 22.2 1.0 CB B:PRO9 5.0 21.8 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