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

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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

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