Zinc in PDB 2afw: Crystal Structure of Human Glutaminyl Cyclase in Complex with N- Acetylhistamine

All present enzymatic activity of Crystal Structure of Human Glutaminyl Cyclase in Complex with N- Acetylhistamine:
2.3.2.5;

The structure of Crystal Structure of Human Glutaminyl Cyclase in Complex with N- Acetylhistamine, PDB code: 2afw 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)	50.00 / 1.56
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	119.132, 119.132, 332.826, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 21.3

The binding sites of Zinc atom in the Crystal Structure of Human Glutaminyl Cyclase in Complex with N- Acetylhistamine (pdb code 2afw). 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 N- Acetylhistamine, PDB code: 2afw:
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 N- Acetylhistamine


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 N- Acetylhistamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn996 b:15.1 occ:1.00 OE2 A:GLU202 2.0 15.2 1.0 NE2 A:AHN1501 2.0 15.8 1.0 OD2 A:ASP159 2.0 14.7 1.0 NE2 A:HIS330 2.1 12.8 1.0 CD A:GLU202 2.7 15.1 1.0 CG A:ASP159 2.8 16.2 1.0 OD1 A:ASP159 2.8 15.5 1.0 OE1 A:GLU202 2.8 15.4 1.0 CE1 A:AHN1501 3.0 17.0 1.0 CD2 A:HIS330 3.0 16.9 1.0 CD2 A:AHN1501 3.0 19.9 1.0 CE1 A:HIS330 3.1 14.6 1.0 O A:HOH542 4.0 15.6 1.0 NE1 A:TRP329 4.0 14.6 1.0 ND1 A:AHN1501 4.1 18.1 1.0 CG A:AHN1501 4.1 19.4 1.0 CG A:HIS330 4.1 14.0 1.0 CG A:GLU202 4.2 14.0 1.0 ND1 A:HIS330 4.2 15.2 1.0 CB A:ASP159 4.2 14.0 1.0 OE1 A:GLU201 4.4 18.6 1.0 O A:HOH538 4.5 15.2 1.0 CD2 A:LEU249 4.6 14.0 1.0 CD1 A:TRP329 4.6 15.7 1.0 NE2 A:HIS140 4.7 13.7 1.0 CE2 A:TRP329 4.8 14.3 1.0 CD A:LYS144 5.0 16.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Glutaminyl Cyclase in Complex with N- Acetylhistamine


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 N- Acetylhistamine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn997 b:16.4 occ:1.00 OE2 B:GLU202 1.9 16.4 1.0 NE2 B:AHN2501 2.0 16.8 1.0 OD2 B:ASP159 2.0 14.2 1.0 NE2 B:HIS330 2.0 17.7 1.0 CD B:GLU202 2.8 16.8 1.0 CG B:ASP159 2.8 14.0 1.0 OE1 B:GLU202 2.9 17.2 1.0 OD1 B:ASP159 2.9 15.5 1.0 CE1 B:AHN2501 2.9 19.2 1.0 CD2 B:HIS330 3.0 16.1 1.0 CD2 B:AHN2501 3.0 22.9 1.0 CE1 B:HIS330 3.1 18.1 1.0 NE1 B:TRP329 4.0 19.0 1.0 O B:HOH470 4.0 14.8 1.0 ND1 B:AHN2501 4.0 20.5 1.0 CG B:AHN2501 4.1 21.2 1.0 CG B:HIS330 4.1 17.3 1.0 ND1 B:HIS330 4.2 18.1 1.0 CG B:GLU202 4.2 14.8 1.0 CB B:ASP159 4.2 14.7 1.0 OE1 B:GLU201 4.3 23.5 1.0 O B:HOH466 4.5 16.9 1.0 CD2 B:LEU249 4.6 16.9 1.0 CD1 B:TRP329 4.6 20.0 1.0 CE2 B:TRP329 4.7 20.0 1.0 NE2 B:HIS140 4.8 14.3 1.0 CD B:LYS144 4.9 16.6 1.0 OE2 B:GLU201 4.9 30.7 1.0 CZ2 B:TRP329 4.9 21.0 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