Zinc in PDB 2zeh: Crystal Structure of the Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution

All present enzymatic activity of Crystal Structure of the Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution:
2.3.2.5;

The structure of Crystal Structure of the Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution, PDB code: 2zeh was solved by K.F.Huang, Y.R.Wang, E.C.Chang, T.L.Chou, A.H.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.80
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	119.051, 119.051, 332.652, 90.00, 90.00, 120.00
R / Rfree (%)	18.1 / 20.7

The binding sites of Zinc atom in the Crystal Structure of the Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution (pdb code 2zeh). 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 Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution, PDB code: 2zeh:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution


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 Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn391 b:20.0 occ:1.00 OE2 A:GLU202 2.0 19.6 1.0 OD2 A:ASP159 2.0 18.3 1.0 O A:HOH401 2.0 29.1 1.0 NE2 A:HIS330 2.1 16.1 1.0 CD A:GLU202 2.7 20.7 1.0 CG A:ASP159 2.8 19.2 1.0 OD1 A:ASP159 2.8 18.7 1.0 OE1 A:GLU202 2.9 20.0 1.0 CD2 A:HIS330 3.0 17.4 1.0 CE1 A:HIS330 3.2 18.8 1.0 O A:HOH540 4.0 16.9 1.0 O A:HOH734 4.1 42.2 1.0 CG A:GLU202 4.2 19.5 1.0 CG A:HIS330 4.2 16.8 1.0 NE1 A:TRP329 4.2 16.6 1.0 CB A:ASP159 4.2 16.4 1.0 ND1 A:HIS330 4.3 17.1 1.0 OE1 A:GLN201 4.3 21.0 1.0 O A:HOH536 4.5 16.9 1.0 O A:HOH813 4.6 34.3 1.0 CD1 A:TRP329 4.7 18.4 1.0 NE2 A:HIS140 4.7 16.3 1.0 CD2 A:LEU249 4.8 18.0 1.0 CE1 A:HIS140 4.9 15.3 1.0 O A:ASP159 4.9 17.2 1.0 CE2 A:TRP329 5.0 16.0 1.0 CD A:LYS144 5.0 21.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution


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 Human Glutaminyl Cyclase Mutant E201Q at 1.8 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn392 b:21.9 occ:1.00 OE2 B:GLU202 2.0 19.2 1.0 NE2 B:HIS330 2.0 20.9 1.0 OD2 B:ASP159 2.0 20.6 1.0 O B:HOH402 2.1 26.4 1.0 CD B:GLU202 2.7 20.4 1.0 CG B:ASP159 2.8 21.1 1.0 OE1 B:GLU202 2.9 20.3 1.0 CD2 B:HIS330 2.9 21.2 1.0 CE1 B:HIS330 3.0 22.9 1.0 OD1 B:ASP159 3.1 20.8 1.0 O B:HOH1095 3.7 35.5 1.0 O B:HOH469 4.0 17.7 1.0 CG B:HIS330 4.1 22.1 1.0 ND1 B:HIS330 4.1 22.4 1.0 NE1 B:TRP329 4.2 23.8 1.0 CG B:GLU202 4.2 18.4 1.0 CB B:ASP159 4.2 18.6 1.0 OE1 B:GLN201 4.2 21.7 1.0 O B:HOH465 4.5 21.2 1.0 CD1 B:TRP329 4.8 25.0 1.0 CE2 B:TRP329 4.8 24.0 1.0 CD B:LYS144 4.8 20.9 1.0 NE2 B:HIS140 4.8 19.9 1.0 CD2 B:LEU249 4.9 21.3 1.0 O B:ASP159 5.0 21.3 1.0

K.F.Huang, Y.R.Wang, E.C.Chang, T.L.Chou, A.H.Wang. A Conserved Hydrogen-Bond Network in the Catalytic Centre of Animal Glutaminyl Cyclases Is Critical For Catalysis. Biochem.J. V. 411 181 2008.
ISSN: ISSN 0264-6021
PubMed: 18072935
DOI: 10.1042/BJ20071073