Chlorine in PDB 6g2a: Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm

Enzymatic activity of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm

All present enzymatic activity of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm:
3.2.2.19;

Protein crystallography data

The structure of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm, PDB code: 6g2a was solved by A.Ariza, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	78.09 / 1.80
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	98.526, 42.940, 89.231, 90.00, 118.93, 90.00
*R / R_free (%)*	18.1 / 22

Other elements in 6g2a:

The structure of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm (pdb code 6g2a). 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 Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm, PDB code: 6g2a:

Chlorine binding site 1 out of 1 in 6g2a

Go back to

Chlorine Binding Sites List in 6g2a

Chlorine binding site 1 out of 1 in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl404 b:47.2 occ:1.00	O	A:HOH511	2.7	28.0	1.0
	N	A:LEU43	2.8	31.6	1.0
	NE2	A:HIS294	2.9	31.2	1.0
	O	A:HOH624	3.0	46.7	1.0
	CA	A:GLY42	3.4	33.3	1.0
	C	A:GLY42	3.6	31.8	1.0
	CB	A:LEU43	3.6	30.3	1.0
	CE1	A:HIS294	3.7	32.6	1.0
	CD2	A:LEU37	3.7	28.8	1.0
	CA	A:LEU43	3.8	30.6	1.0
	CG	A:LEU37	4.0	29.1	1.0
	CD2	A:HIS294	4.0	29.4	1.0
	OXT	A:ACT405	4.1	42.4	1.0
	CD1	A:LEU37	4.4	28.3	1.0
	C	A:ACT405	4.4	43.4	1.0
	CE	A:LYS290	4.5	38.6	1.0
	CH3	A:ACT405	4.6	45.5	1.0
	O	A:GLY42	4.8	31.1	1.0
	CD	A:LYS290	4.8	38.3	1.0
	N	A:GLY42	4.8	33.6	1.0
	ND1	A:HIS294	4.9	31.9	1.0
	CG	A:LYS290	5.0	35.7	1.0

Reference:

J.G.M.Rack, A.Ariza, B.S.Drown, C.Henfrey, E.Bartlett, T.Shirai, P.J.Hergenrother, I.Ahel. (Adp-Ribosyl)Hydrolases: Structural Basis For Differential Substrate Recognition and Inhibition. Cell Chem Biol V. 25 1533 2018.
ISSN: ESSN 2451-9448
PubMed: 30472116
DOI: 10.1016/J.CHEMBIOL.2018.11.001

Page generated: Sat Jul 12 14:20:07 2025

Last articles

Mg in 5E6S
Mg in 5E75
Mg in 5E6U
Mg in 5E67
Mg in 5E6F
Mg in 5E6R
Mg in 5E54
Mg in 5E63
Mg in 5E5A
Mg in 5E5S

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