Chlorine in PDB 3hfw: Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1)

All present enzymatic activity of Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1):
3.2.2.19;

The structure of Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1), PDB code: 3hfw was solved by C.Mueller-Dieckmann, M.S.Weiss, J.Mueller-Dieckmann, F.Koch-Nolte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.92
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.280, 52.790, 140.340, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 18.5

The structure of Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1) also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Potassium	(K)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1) (pdb code 3hfw). 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 Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1), PDB code: 3hfw:

Chlorine binding site 1 out of 1 in the Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Adp-Ribosylhydrolase 1 (HARH1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl360 b:24.1 occ:1.00 NE2 A:HIS294 3.0 4.8 1.0 O A:HOH439 3.0 11.2 1.0 N A:LEU43 3.2 9.3 1.0 CE1 A:HIS294 3.7 8.6 1.0 CA A:GLY42 3.8 10.8 1.0 CB A:LEU43 3.8 8.9 1.0 CD2 A:LEU37 3.9 3.2 1.0 CE A:LYS290 3.9 20.4 1.0 C A:GLY42 4.0 10.5 1.0 CD2 A:HIS294 4.1 11.3 1.0 CA A:LEU43 4.1 9.6 1.0 CG A:LEU37 4.4 8.1 1.0 CG A:LYS290 4.5 16.9 1.0 CD A:LYS290 4.6 12.3 1.0 NZ A:LYS290 4.7 18.0 1.0 CD1 A:LEU37 4.8 8.1 1.0 ND1 A:HIS294 4.9 7.1 1.0 O A:HOH431 5.0 19.7 1.0

F.Koch-Nolte, J.Mueller-Dieckmann, M.S.Weiss, C.Mueller-Dieckmann. Crystal Structure of Human Adp-Ribosylhydrolase 1 To Be Published.