Zinc 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:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Structure of Glycosylated Human Glutaminyl Cyclase (pdb code 3si0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Glycosylated Human Glutaminyl Cyclase, PDB code: 3si0:

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Glycosylated Human Glutaminyl Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn362 b:19.4 occ:1.00 N3 A:IMD363 1.8 12.6 1.0 OD1 A:ASP159 2.0 23.7 1.0 OE2 A:GLU202 2.0 17.5 1.0 NE2 A:HIS330 2.1 19.7 1.0 OD2 A:ASP159 2.5 17.9 1.0 CG A:ASP159 2.6 18.5 1.0 CD2 A:HIS330 2.8 20.3 1.0 C4 A:IMD363 2.9 15.8 1.0 C2 A:IMD363 2.9 13.9 1.0 CD A:GLU202 2.9 18.6 1.0 OE1 A:GLU202 3.2 17.9 1.0 CE1 A:HIS330 3.3 22.8 1.0 NE1 A:TRP329 3.7 25.9 1.0 O A:HOH365 3.9 2.0 1.0 N1 A:IMD363 4.0 18.0 1.0 C5 A:IMD363 4.0 18.9 1.0 CG A:HIS330 4.1 23.7 1.0 CB A:ASP159 4.1 18.8 1.0 ND1 A:HIS330 4.3 22.6 1.0 CD1 A:TRP329 4.3 24.6 1.0 CG A:GLU202 4.4 16.7 1.0 CE2 A:TRP329 4.4 23.5 1.0 OE1 A:GLU201 4.4 26.0 1.0 O A:HOH6 4.5 5.0 1.0 CD2 A:LEU249 4.6 20.0 1.0 NE2 A:HIS140 4.7 21.1 1.0 CZ2 A:TRP329 4.8 25.3 1.0 CD A:LYS144 4.9 20.7 1.0 O A:ASP159 5.0 17.4 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