Chlorine in PDB 3si0: Structure of Glycosylated Human Glutaminyl Cyclase

All present enzymatic activity of Structure of Glycosylated Human Glutaminyl Cyclase:
2.3.2.5;

The structure of Structure of Glycosylated Human Glutaminyl Cyclase, PDB code: 3si0 was solved by C.Parthier, D.Carrillo, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	11.98 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	82.408, 63.688, 77.159, 90.00, 105.76, 90.00
R / Rfree (%)	20.4 / 26.4

The structure of Structure of Glycosylated Human Glutaminyl Cyclase also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Structure of Glycosylated Human Glutaminyl Cyclase (pdb code 3si0). 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 Structure of Glycosylated Human Glutaminyl Cyclase, PDB code: 3si0:

Chlorine binding site 1 out of 1 in the Structure of Glycosylated Human Glutaminyl Cyclase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Glycosylated Human Glutaminyl Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl364 b:25.2 occ:0.50 CA A:SER81 2.9 22.6 1.0 NH2 A:ARG118 2.9 19.9 1.0 N A:SER81 3.2 25.1 1.0 OH A:TYR78 3.3 26.9 1.0 CB A:SER81 3.5 22.9 1.0 C A:GLY80 3.5 24.8 1.0 O A:GLY80 3.5 25.8 1.0 CE2 A:TYR78 3.5 27.6 1.0 CZ A:TYR78 3.7 26.8 1.0 CZ A:ARG118 4.0 25.4 1.0 CD A:PRO82 4.2 22.5 1.0 C A:SER81 4.2 22.8 1.0 NH1 A:ARG118 4.4 21.4 1.0 CD2 A:TYR78 4.6 27.6 1.0 CA A:GLY80 4.6 25.1 1.0 N A:PRO82 4.7 21.7 1.0 O A:PRO79 4.7 26.7 1.0 OG A:SER81 4.9 21.2 1.0 CE1 A:TYR78 4.9 26.8 1.0

D.Ruiz-Carrillo, B.Koch, C.Parthier, M.Wermann, T.Dambe, M.Buchholz, H.H.Ludwig, U.Heiser, J.U.Rahfeld, M.T.Stubbs, S.Schilling, H.U.Demuth. Structures of Glycosylated Mammalian Glutaminyl Cyclases Reveal Conformational Variability Near the Active Center. Biochemistry V. 50 6280 2011.
ISSN: ISSN 0006-2960
PubMed: 21671571
DOI: 10.1021/BI200249H