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Chlorine in PDB 5nru: Cys-Gly Dipeptidase Glij in Complex with ZN2+

Enzymatic activity of Cys-Gly Dipeptidase Glij in Complex with ZN2+

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

Protein crystallography data

The structure of Cys-Gly Dipeptidase Glij in Complex with ZN2+, PDB code: 5nru 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 / 2.15
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 99.210, 99.210, 106.670, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 21.1

Other elements in 5nru:

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

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Cys-Gly Dipeptidase Glij in Complex with ZN2+ (pdb code 5nru). 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 Cys-Gly Dipeptidase Glij in Complex with ZN2+, PDB code: 5nru:

Chlorine binding site 1 out of 1 in 5nru

Go back to Chlorine Binding Sites List in 5nru
Chlorine binding site 1 out of 1 in the Cys-Gly Dipeptidase Glij in Complex with 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 ZN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:71.3
occ:1.00
N A:ASP363 4.1 70.9 1.0
CG A:ASP363 4.3 81.5 1.0
OD2 A:ASP363 4.3 81.5 1.0
CD2 A:LEU362 4.4 55.1 1.0
CA A:LEU362 4.4 65.8 1.0
OD1 A:ASP363 4.6 83.0 1.0
CB A:ASP363 4.6 79.2 1.0
CB A:LEU362 4.8 62.2 1.0
C A:LEU362 4.8 67.0 1.0
O A:GLU361 4.8 70.0 1.0

Reference:

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
Page generated: Sat Dec 12 12:10:27 2020

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