Atomistry » Chlorine » PDB 1xkk-1y6p » 1xv5
Atomistry »
  Chlorine »
    PDB 1xkk-1y6p »
      1xv5 »

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

Enzymatic activity of Alpha-Glucosyltransferase (Agt) in Complex with Udp

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

Protein crystallography data

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

Chlorine Binding Sites:

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 1xv5

Go back to Chlorine Binding Sites List in 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

Reference:

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
Page generated: Sat Dec 12 08:54:57 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy