Zinc in PDB 2afo: Crystal Structure of Human Glutaminyl Cyclase at pH 8.0

All present enzymatic activity of Crystal Structure of Human Glutaminyl Cyclase at pH 8.0:
2.3.2.5;

The structure of Crystal Structure of Human Glutaminyl Cyclase at pH 8.0, PDB code: 2afo 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 / 2.35
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	118.988, 118.988, 332.258, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 21.6

The binding sites of Zinc atom in the Crystal Structure of Human Glutaminyl Cyclase at pH 8.0 (pdb code 2afo). 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 at pH 8.0, PDB code: 2afo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human Glutaminyl Cyclase at pH 8.0


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 at pH 8.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn391 b:28.9 occ:1.00 OD2 A:ASP159 1.8 28.5 1.0 OE2 A:GLU202 1.9 26.8 1.0 NE2 A:HIS330 2.1 30.7 1.0 O A:HOH401 2.3 30.3 1.0 CD A:GLU202 2.7 26.1 1.0 CG A:ASP159 2.8 28.5 1.0 OE1 A:GLU202 2.9 26.5 1.0 CD2 A:HIS330 2.9 30.5 1.0 OD1 A:ASP159 3.1 27.4 1.0 CE1 A:HIS330 3.2 30.9 1.0 CG A:GLU202 4.1 26.3 1.0 CG A:HIS330 4.1 31.3 1.0 NE1 A:TRP329 4.1 22.4 1.0 CB A:ASP159 4.2 26.3 1.0 O A:HOH530 4.2 26.1 1.0 ND1 A:HIS330 4.2 31.9 1.0 OE1 A:GLU201 4.4 30.4 1.0 CD2 A:LEU249 4.5 21.6 1.0 O A:HOH526 4.6 20.9 1.0 CD1 A:TRP329 4.7 23.0 1.0 NE2 A:HIS140 4.8 26.5 1.0 O A:HOH573 4.8 54.4 1.0 CE2 A:TRP329 5.0 22.7 1.0 O A:ASP159 5.0 26.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Glutaminyl Cyclase at pH 8.0


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 at pH 8.0 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn392 b:33.2 occ:1.00 OE2 B:GLU202 1.8 25.9 1.0 OD2 B:ASP159 1.9 30.2 1.0 NE2 B:HIS330 2.1 31.8 1.0 O B:HOH402 2.4 33.0 1.0 CD B:GLU202 2.8 27.1 1.0 CG B:ASP159 2.9 31.2 1.0 CD2 B:HIS330 2.9 32.6 1.0 OE1 B:GLU202 3.1 28.4 1.0 CE1 B:HIS330 3.1 32.5 1.0 OD1 B:ASP159 3.2 32.6 1.0 NE1 B:TRP329 4.0 32.9 1.0 O B:HOH464 4.1 28.6 1.0 CG B:HIS330 4.1 33.7 1.0 CG B:GLU202 4.1 26.2 1.0 ND1 B:HIS330 4.2 33.9 1.0 CB B:ASP159 4.2 30.5 1.0 O B:HOH461 4.4 33.5 1.0 OE1 B:GLU201 4.6 31.1 1.0 CE2 B:TRP329 4.6 32.8 1.0 CD2 B:LEU249 4.7 30.9 1.0 CD1 B:TRP329 4.7 34.2 1.0 CD B:LYS144 4.9 26.7 1.0 CZ2 B:TRP329 4.9 32.7 1.0 NE2 B:HIS140 4.9 28.0 1.0 CB B:LYS144 5.0 28.2 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