Zinc in PDB 2afu: Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester

All present enzymatic activity of Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester:
2.3.2.5;

The structure of Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester, PDB code: 2afu was solved by K.F.Huang, Y.L.Liu, W.J.Cheng, T.P.Ko, A.H.J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.22
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	119.137, 119.137, 332.612, 90.00, 90.00, 120.00
R / Rfree (%)	18.8 / 22.6

The binding sites of Zinc atom in the Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester (pdb code 2afu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester, PDB code: 2afu:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn391 b:28.9 occ:1.00 OE2 A:GLU202 2.0 26.2 1.0 OD2 A:ASP159 2.0 28.7 1.0 N A:BGT381 2.1 41.4 1.0 NE2 A:HIS330 2.1 26.1 1.0 CD A:GLU202 2.8 24.9 1.0 O A:BGT381 2.9 43.5 1.0 CG A:ASP159 2.9 28.6 1.0 OE1 A:GLU202 2.9 24.4 1.0 CD2 A:HIS330 3.0 25.7 1.0 OD1 A:ASP159 3.1 29.1 1.0 CE1 A:HIS330 3.2 24.1 1.0 CA A:BGT381 3.3 42.6 1.0 C A:BGT381 3.5 43.0 1.0 O A:HOH533 4.0 22.8 1.0 CB A:BGT381 4.0 41.5 1.0 OE1 A:GLN201 4.1 29.6 1.0 CG A:HIS330 4.2 26.7 1.0 CG A:GLU202 4.2 24.6 1.0 ND1 A:HIS330 4.2 27.1 1.0 CB A:ASP159 4.3 27.2 1.0 NE1 A:TRP329 4.3 22.9 1.0 O A:HOH529 4.7 22.3 1.0 CD2 A:LEU249 4.7 25.4 1.0 OXT A:BGT381 4.7 43.1 1.0 CD1 A:TRP329 4.9 23.8 1.0 NE2 A:HIS140 4.9 25.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn392 b:26.9 occ:1.00 OE2 B:GLU202 1.8 22.1 1.0 OD2 B:ASP159 1.9 25.2 1.0 NE2 B:HIS330 2.1 24.6 1.0 O B:HOH401 2.4 29.9 1.0 CD B:GLU202 2.7 21.6 1.0 CG B:ASP159 2.9 24.8 1.0 OE1 B:GLU202 2.9 22.0 1.0 CD2 B:HIS330 2.9 24.6 1.0 OD1 B:ASP159 3.1 24.4 1.0 CE1 B:HIS330 3.1 24.6 1.0 NE1 B:TRP329 4.0 22.6 1.0 CG B:GLU202 4.1 21.0 1.0 O B:HOH467 4.1 22.7 1.0 CG B:HIS330 4.1 25.5 1.0 ND1 B:HIS330 4.2 24.8 1.0 CB B:ASP159 4.2 23.4 1.0 OE1 B:BGT382 4.3 39.7 1.0 OE1 B:GLN201 4.4 28.7 1.0 O B:HOH463 4.5 27.4 1.0 CD2 B:LEU249 4.6 21.5 1.0 CE2 B:TRP329 4.7 23.2 1.0 CD1 B:TRP329 4.8 24.1 1.0 CZ2 B:TRP329 4.9 22.7 1.0 CD B:LYS144 5.0 20.8 1.0 NE2 B:HIS140 5.0 22.3 1.0 O B:HOH609 5.0 20.5 1.0

K.F.Huang, Y.L.Liu, W.J.Cheng, T.P.Ko, A.H.Wang. Crystal Structures of Human Glutaminyl Cyclase, An Enzyme Responsible For Protein N-Terminal Pyroglutamate Formation Proc.Natl.Acad.Sci.Usa V. 102 13117 2005.
ISSN: ISSN 0027-8424
PubMed: 16135565
DOI: 10.1073/PNAS.0504184102