Chlorine in PDB 6g28: Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose

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

The structure of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose, PDB code: 6g28 was solved by A.Ariza, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.09 / 1.23
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.102, 66.687, 83.420, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 15.7

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

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose (pdb code 6g28). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose, PDB code: 6g28:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose


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-Ribose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:43.4 occ:1.00 O A:HOH797 2.7 41.7 1.0 O A:HOH790 2.8 34.9 1.0 NE2 A:HIS294 2.8 27.4 1.0 N A:LEU43 2.9 26.2 1.0 CA A:GLY42 3.4 29.0 1.0 CD2 A:LEU37 3.6 26.1 1.0 CE1 A:HIS294 3.6 28.3 1.0 C A:GLY42 3.6 27.0 1.0 CB A:LEU43 3.7 24.9 1.0 CG A:LEU37 3.9 26.1 1.0 CA A:LEU43 3.9 24.9 1.0 CD2 A:HIS294 3.9 25.9 1.0 O A:HOH769 4.1 34.7 1.0 CD1 A:LEU37 4.3 25.4 1.0 O A:HOH823 4.6 40.1 1.0 O A:HOH531 4.6 40.4 1.0 N A:GLY42 4.8 29.7 1.0 CD A:LYS290 4.8 31.9 1.0 ND1 A:HIS294 4.8 28.0 1.0 CG A:LYS290 4.9 29.4 1.0 O A:GLY42 4.9 25.9 1.0 CE A:LYS290 4.9 32.4 1.0 O A:HOH645 5.0 32.3 0.5

Chlorine binding site 2 out of 3 in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:32.7 occ:1.00 N A:ARG336 3.1 18.6 1.0 CL A:CL406 3.1 37.6 1.0 CA A:TYR333 3.4 15.4 1.0 CB A:ARG336 3.4 18.3 1.0 C A:TYR333 3.5 15.4 1.0 N A:ASN335 3.5 18.8 1.0 CB A:ASN335 3.6 21.1 0.5 O A:TYR333 3.7 15.7 1.0 CB A:ASN335 3.8 21.4 0.5 CA A:ARG336 3.8 17.9 1.0 CA A:ASN335 3.9 20.0 0.5 CA A:ASN335 3.9 20.0 0.5 C A:ASN335 3.9 19.3 1.0 N A:ARG334 4.0 16.4 1.0 N A:TYR333 4.2 14.6 1.0 O A:HOH726 4.3 25.6 1.0 C A:ARG334 4.4 18.2 1.0 CD1 A:TYR333 4.4 17.3 1.0 CB A:TYR333 4.4 15.1 1.0 CG A:ASN335 4.6 22.4 0.5 ND2 A:ASN335 4.8 23.7 0.5 CG A:ARG336 4.8 18.2 1.0 CA A:ARG334 4.8 17.7 1.0 CG A:ASN335 4.9 23.0 0.5 OD1 A:ASN335 4.9 24.3 0.5 CD A:ARG336 5.0 19.1 1.0 CG A:TYR333 5.0 15.4 1.0

Chlorine binding site 3 out of 3 in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Ribose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl406 b:37.6 occ:1.00 O A:HOH574 2.8 29.8 1.0 N A:ASN335 3.0 18.8 1.0 CL A:CL405 3.1 32.7 1.0 CG A:ASN335 3.3 22.4 0.5 N A:ARG334 3.4 16.4 1.0 CB A:ASN335 3.5 21.1 0.5 CB A:ASN335 3.5 21.4 0.5 OD1 A:ASN335 3.5 24.3 0.5 CA A:ASN335 3.8 20.0 0.5 ND2 A:ASN335 3.8 23.1 0.5 CA A:ASN335 3.8 20.0 0.5 C A:ARG334 3.9 18.2 1.0 CA A:ARG334 3.9 17.7 1.0 CB A:ARG334 4.0 19.8 1.0 C A:TYR333 4.0 15.4 1.0 O A:HOH726 4.1 25.6 1.0 CA A:TYR333 4.4 15.4 1.0 N A:TYR333 4.4 14.6 1.0 O A:LEU331 4.4 15.8 1.0 O A:TYR333 4.7 15.7 1.0 N A:ARG336 4.8 18.6 1.0 C A:ASN335 4.9 19.3 1.0 CG A:ASN335 5.0 23.0 0.5

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