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

Go back to

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: Sat Jul 20 04:07:43 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy