Chlorine in PDB 1xv5: Alpha-Glucosyltransferase (Agt) in Complex with Udp

All present enzymatic activity of Alpha-Glucosyltransferase (Agt) in Complex with Udp:
2.4.1.26;

The structure of Alpha-Glucosyltransferase (Agt) in Complex with Udp, PDB code: 1xv5 was solved by L.Lariviere, N.Sommer, S.Morera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.73
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.806, 68.241, 65.750, 90.00, 109.10, 90.00
R / Rfree (%)	17.5 / 20.5

The binding sites of Chlorine atom in the Alpha-Glucosyltransferase (Agt) in Complex with Udp (pdb code 1xv5). 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 Alpha-Glucosyltransferase (Agt) in Complex with Udp, PDB code: 1xv5:

Chlorine binding site 1 out of 1 in the Alpha-Glucosyltransferase (Agt) in Complex with Udp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Alpha-Glucosyltransferase (Agt) in Complex with Udp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1401 b:34.4 occ:1.00 O A:HOH447 2.6 20.6 1.0 N A:CME1014 2.9 18.2 1.0 N A:THR1017 3.2 14.5 1.0 C A:CME1014 3.2 16.2 1.0 N A:VAL1016 3.2 13.3 1.0 CA A:CME1014 3.3 18.4 1.0 O A:CME1014 3.4 15.8 1.0 CB A:CME1014 3.5 21.2 1.0 CB A:GLU1012 3.5 28.6 1.0 CB A:VAL1016 3.5 14.9 1.0 OG1 A:THR1017 3.6 15.7 1.0 N A:GLY1015 3.6 16.4 1.0 CA A:VAL1016 3.7 14.2 1.0 N A:GLY1013 3.8 21.7 1.0 CB A:THR1017 3.9 17.0 1.0 C A:VAL1016 3.9 14.2 1.0 C2 A:EDO1403 4.0 34.0 1.0 C A:GLY1013 4.1 18.7 1.0 C A:GLU1012 4.1 24.1 1.0 C A:GLY1015 4.1 15.4 1.0 CA A:THR1017 4.1 15.3 1.0 CA A:GLU1012 4.2 24.5 1.0 CG2 A:VAL1016 4.2 16.2 1.0 CG A:GLU1012 4.3 35.7 1.0 OE2 A:GLU1012 4.4 41.1 1.0 CA A:GLY1015 4.4 14.8 1.0 N A:GLU1012 4.4 23.5 1.0 CA A:GLY1013 4.4 19.4 1.0 O2 A:EDO1403 4.6 32.1 1.0 CG1 A:VAL1016 4.7 17.5 1.0 CD A:GLU1012 4.7 38.6 1.0 SD A:CME1014 4.8 38.8 1.0 O A:HOH94 4.9 20.7 1.0 O A:GLU1012 4.9 24.2 1.0 SG A:CME1014 4.9 27.5 1.0

L.Lariviere, N.Sommer, S.Morera. Structural Evidence of A Passive Base-Flipping Mechanism For Agt, An Unusual Gt-B Glycosyltransferase. J.Mol.Biol. V. 352 139 2005.
ISSN: ISSN 0022-2836
PubMed: 16081100
DOI: 10.1016/J.JMB.2005.07.007