Chlorine in PDB 1y6g: Alpha-Glucosyltransferase in Complex with Udp and A 13_MER Dna Containing A Hmu Base at 2.8 A Resolution

Enzymatic activity of Alpha-Glucosyltransferase in Complex with Udp and A 13_MER Dna Containing A Hmu Base at 2.8 A Resolution

All present enzymatic activity of Alpha-Glucosyltransferase in Complex with Udp and A 13_MER Dna Containing A Hmu Base at 2.8 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 2.8 A Resolution, PDB code: 1y6g 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 / 2.80
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	46.994, 120.520, 86.807, 90.00, 94.68, 90.00
*R / R_free (%)*	21.9 / 28.7

Other elements in 1y6g:

The structure of Alpha-Glucosyltransferase in Complex with Udp and A 13_MER Dna Containing A Hmu Base at 2.8 A Resolution also contains other interesting chemical elements:

Cobalt

(Co)

7 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 2.8 A Resolution (pdb code 1y6g). 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 2.8 A Resolution, PDB code: 1y6g:

Chlorine binding site 1 out of 1 in 1y6g

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Chlorine Binding Sites List in 1y6g

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 2.8 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 2.8 A Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cl2017 b:65.2 occ:1.00	N2	B:NCO2019	3.0	99.6	0.5
	N1	B:NCO2019	3.4	100.0	0.5
	ND1	B:HIS1114	3.5	30.8	1.0
	NE2	B:HIS1140	3.9	38.9	1.0
	CE1	B:HIS1140	4.1	37.8	1.0
	CB	B:PRO1176	4.2	39.5	1.0
	C	B:GLY1015	4.2	32.8	1.0
	CA	B:GLY1015	4.2	34.0	1.0
	O	B:GLY1015	4.3	30.6	1.0
	CG	B:PRO1176	4.3	41.2	1.0
	CO	B:NCO2019	4.3	100.0	0.5
	CE1	B:HIS1114	4.4	29.7	1.0
	O1A	B:UDP2021	4.4	40.6	1.0
	O	B:HOH2054	4.5	39.8	1.0
	CG	B:HIS1114	4.5	31.0	1.0
	N3	B:NCO2019	4.5	98.8	0.5
	CB	B:HIS1114	4.7	33.3	1.0
	O	B:HIS1114	4.7	37.5	1.0
	N	B:VAL1016	4.7	32.7	1.0
	CE1	B:TYR1307	4.8	26.3	1.0
	N6	B:NCO2019	4.9	98.5	0.5
	CD1	B:TYR1307	5.0	28.0	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: Thu Jul 10 20:32:30 2025

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