Chlorine in PDB 5ns5: Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+

All present enzymatic activity of Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+:
3.4.13.19;

The structure of Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+, PDB code: 5ns5 was solved by M.Groll, E.M.Huber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	99.000, 99.000, 106.490, 90.00, 90.00, 120.00
R / Rfree (%)	17.7 / 18.9

The structure of Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+ also contains other interesting chemical elements:

Copper	(Cu)	2 atoms
Zinc	(Zn)	2 atoms

The binding sites of Chlorine atom in the Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+ (pdb code 5ns5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+, PDB code: 5ns5:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:74.4 occ:1.00 O A:ASP239 3.2 47.2 1.0 CB A:ASP239 4.0 47.9 1.0 C A:ASP239 4.0 47.1 1.0 CB A:HIS243 4.1 49.9 1.0 CA A:ASP239 4.3 46.9 1.0 N A:HIS243 4.4 46.8 1.0 CG A:ASP239 4.7 50.0 1.0 CA A:HIS243 4.7 47.0 1.0 CB A:LEU242 4.8 46.0 1.0 CG2 A:ILE284 4.8 47.2 1.0 OD2 A:ASP239 4.9 50.2 1.0

Chlorine binding site 2 out of 3 in the Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl406 b:72.0 occ:1.00 NH1 A:ARG123 3.2 80.5 1.0 O A:HOH553 3.8 78.8 1.0 CE2 A:TRP119 4.2 47.7 1.0 CD2 A:TRP119 4.3 47.3 1.0 NE1 A:TRP119 4.3 48.5 1.0 CZ A:ARG123 4.5 79.7 1.0 CG A:TRP119 4.5 46.8 1.0 CD1 A:TRP119 4.5 47.8 1.0 CZ2 A:TRP119 4.6 48.3 1.0 O A:HOH669 4.7 58.3 1.0 CE3 A:TRP119 4.7 48.0 1.0 CH2 A:TRP119 5.0 49.1 1.0

Chlorine binding site 3 out of 3 in the Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Cys-Gly Dipeptidase Glij in Complex with CU2+ and ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl407 b:71.5 occ:1.00 C A:MET298 4.7 55.5 1.0 N A:LEU299 4.8 56.3 1.0 O A:MET298 4.8 54.9 1.0

A.Marion, M.Groll, D.H.Scharf, K.Scherlach, M.Glaser, H.Sievers, M.Schuster, C.Hertweck, A.A.Brakhage, I.Antes, E.M.Huber. Gliotoxin Biosynthesis: Structure, Mechanism, and Metal Promiscuity of Carboxypeptidase Glij. Acs Chem. Biol. V. 12 1874 2017.
ISSN: ESSN 1554-8937
PubMed: 28525266
DOI: 10.1021/ACSCHEMBIO.6B00847