Zinc in PDB 2afs: Crystal Structure of the Genetic Mutant R54W of Human Glutaminyl Cyclase

All present enzymatic activity of Crystal Structure of the Genetic Mutant R54W of Human Glutaminyl Cyclase:
2.3.2.5;

The structure of Crystal Structure of the Genetic Mutant R54W of Human Glutaminyl Cyclase, PDB code: 2afs 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 (°)	119.447, 119.447, 333.848, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 22.2

The binding sites of Zinc atom in the Crystal Structure of the Genetic Mutant R54W of Human Glutaminyl Cyclase (pdb code 2afs). 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 the Genetic Mutant R54W of Human Glutaminyl Cyclase, PDB code: 2afs:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Genetic Mutant R54W of 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 Crystal Structure of the Genetic Mutant R54W of Human Glutaminyl Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn391 b:22.1 occ:1.00 OE2 A:GLU202 1.9 18.7 1.0 OD2 A:ASP159 1.9 19.3 1.0 NE2 A:HIS330 2.1 19.0 1.0 O A:HOH401 2.2 22.2 1.0 CD A:GLU202 2.8 19.2 1.0 CG A:ASP159 2.8 20.3 1.0 CD2 A:HIS330 2.9 20.1 1.0 OE1 A:GLU202 3.0 17.5 1.0 OD1 A:ASP159 3.0 22.7 1.0 CE1 A:HIS330 3.2 19.7 1.0 O A:HOH532 4.1 15.6 1.0 O A:HOH581 4.1 25.7 1.0 CG A:HIS330 4.1 20.9 1.0 CG A:GLU202 4.2 18.2 1.0 ND1 A:HIS330 4.2 20.7 1.0 NE1 A:TRP329 4.2 17.4 1.0 CB A:ASP159 4.2 18.5 1.0 OE1 A:GLU201 4.4 22.8 1.0 O A:HOH528 4.6 20.0 1.0 CD2 A:LEU249 4.6 19.1 1.0 NE2 A:HIS140 4.7 19.5 1.0 CD1 A:TRP329 4.7 19.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Genetic Mutant R54W of Human Glutaminyl Cyclase


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 the Genetic Mutant R54W of Human Glutaminyl Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn392 b:23.4 occ:1.00 OE2 B:GLU202 1.7 19.9 1.0 OD2 B:ASP159 1.9 21.8 1.0 NE2 B:HIS330 2.0 24.5 1.0 O B:HOH402 2.3 29.2 1.0 CD B:GLU202 2.7 20.2 1.0 CG B:ASP159 2.8 22.1 1.0 CD2 B:HIS330 2.9 25.1 1.0 OE1 B:GLU202 3.1 21.3 1.0 OD1 B:ASP159 3.1 21.5 1.0 CE1 B:HIS330 3.1 24.7 1.0 NE1 B:TRP329 4.0 24.5 1.0 O B:HOH464 4.1 18.2 1.0 CG B:GLU202 4.1 19.2 1.0 CG B:HIS330 4.1 25.1 1.0 ND1 B:HIS330 4.1 25.9 1.0 CB B:ASP159 4.2 20.5 1.0 O B:HOH460 4.5 21.5 1.0 OE1 B:GLU201 4.5 27.8 1.0 CD1 B:TRP329 4.6 25.0 1.0 CD2 B:LEU249 4.7 21.4 1.0 CE2 B:TRP329 4.7 24.9 1.0 NE2 B:HIS140 4.9 20.6 1.0 CD B:LYS144 5.0 19.4 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