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Chlorine in PDB 1y8z: Alpha-Glucosyltransferase in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution

Enzymatic activity of Alpha-Glucosyltransferase in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution

All present enzymatic activity of Alpha-Glucosyltransferase in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution:
2.4.1.26;

Protein crystallography data

The structure of Alpha-Glucosyltransferase in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution, PDB code: 1y8z 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 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.263, 114.655, 86.143, 90.00, 89.49, 90.00
R / Rfree (%) 20.8 / 25

Other elements in 1y8z:

The structure of Alpha-Glucosyltransferase in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution also contains other interesting chemical elements:

Cobalt (Co) 5 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Alpha-Glucosyltransferase in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution (pdb code 1y8z). 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 in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution, PDB code: 1y8z:

Chlorine binding site 1 out of 1 in 1y8z

Go back to Chlorine Binding Sites List in 1y8z
Chlorine binding site 1 out of 1 in the Alpha-Glucosyltransferase in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Alpha-Glucosyltransferase in Complex with Udp and A 13-Mer Dna Containing A Hmu Base at 1.9 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl4001

b:36.1
occ:1.00
 O B:HOH489 3.0 22.2 1.0
N B:VAL1016 3.1 19.8 1.0
N B:CME1014 3.1 25.0 1.0
C B:CME1014 3.4 23.1 1.0
N B:THR1017 3.4 17.9 1.0
CB B:CME1014 3.4 29.4 1.0
CB B:VAL1016 3.4 23.0 1.0
CA B:CME1014 3.4 25.6 1.0
CB B:GLU1012 3.5 31.9 1.0
N B:GLY1015 3.5 22.0 1.0
CA B:VAL1016 3.7 20.7 1.0
OG1 B:THR1017 3.8 20.3 1.0
O B:CME1014 3.8 23.6 1.0
CG2 B:VAL1016 3.8 21.5 1.0
N B:GLY1013 4.0 26.7 1.0
C B:VAL1016 4.0 19.4 1.0
C B:GLY1015 4.1 21.6 1.0
CE B:CME1014 4.1 42.1 1.0
CG B:GLU1012 4.2 38.4 1.0
CB B:THR1017 4.3 16.7 1.0
CA B:GLY1015 4.3 22.6 1.0
CA B:GLU1012 4.3 28.6 1.0
C B:GLY1013 4.3 25.9 1.0
OE2 B:GLU1012 4.3 44.7 1.0
C B:GLU1012 4.4 29.3 1.0
CD B:GLU1012 4.4 41.5 1.0
CA B:THR1017 4.4 18.3 1.0
N B:GLU1012 4.6 28.1 1.0
SD B:CME1014 4.6 42.6 1.0
CG1 B:VAL1016 4.7 21.6 1.0
CA B:GLY1013 4.8 25.7 1.0
SG B:CME1014 4.8 33.5 1.0
CZ B:CME1014 4.9 42.6 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 Jul 20 04:09:00 2024

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