Zinc in PDB 6qro: Crystal Structure of Tannerella Forsythia Glutaminyl Cyclase

The structure of Crystal Structure of Tannerella Forsythia Glutaminyl Cyclase, PDB code: 6qro was solved by M.Linnert, A.Piechotta, C.Parthier, N.Taudte, P.Kolenko, J.Rahfeld, J.Potempa, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.92 / 2.10
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	56.070, 79.240, 83.080, 89.94, 90.00, 71.94
R / Rfree (%)	17.4 / 20.1

The binding sites of Zinc atom in the Crystal Structure of Tannerella Forsythia Glutaminyl Cyclase (pdb code 6qro). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Tannerella Forsythia Glutaminyl Cyclase, PDB code: 6qro:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Tannerella Forsythia 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 Tannerella Forsythia Glutaminyl Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:13.5 occ:1.00 O A:HOH512 1.8 8.4 1.0 OD2 A:ASP184 1.9 7.6 1.0 OD2 A:ASP151 1.9 7.9 1.0 OD1 A:ASP184 2.3 13.0 1.0 CG A:ASP184 2.4 8.9 1.0 NE2 A:HIS305 2.6 11.9 1.0 CG A:ASP151 2.7 8.8 1.0 OD1 A:ASP151 2.8 7.8 1.0 CD2 A:HIS305 3.3 9.9 1.0 NE1 A:TRP304 3.5 10.1 1.0 O A:HOH505 3.7 8.3 1.0 CE1 A:HIS305 3.7 8.8 1.0 CB A:ASP184 3.9 8.3 1.0 CB A:ASP151 4.1 9.4 1.0 CE2 A:TRP304 4.2 13.0 1.0 CD1 A:TRP304 4.3 8.8 1.0 OE1 A:GLU183 4.5 11.7 1.0 CZ2 A:TRP304 4.5 12.2 1.0 CG A:HIS305 4.6 9.2 1.0 NE2 A:HIS126 4.7 5.6 1.0 ND1 A:HIS305 4.7 12.1 1.0 OE2 A:GLU183 4.8 8.4 1.0 CA A:ASP184 4.8 10.8 1.0 CD A:ARG130 4.9 9.4 1.0 CZ3 A:TRP199 5.0 11.1 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Tannerella Forsythia 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 Tannerella Forsythia Glutaminyl Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:17.7 occ:1.00 OD2 B:ASP151 1.9 13.5 1.0 NE2 B:HIS305 1.9 16.2 1.0 O B:HOH572 2.0 12.6 1.0 OD2 B:ASP184 2.1 14.9 1.0 OD1 B:ASP184 2.6 11.3 1.0 CD2 B:HIS305 2.6 15.3 1.0 CG B:ASP184 2.7 11.0 1.0 CG B:ASP151 3.0 10.5 1.0 CE1 B:HIS305 3.1 14.4 1.0 NE1 B:TRP304 3.1 15.8 1.0 OD1 B:ASP151 3.5 11.1 1.0 O B:HOH563 3.7 11.3 1.0 CG B:HIS305 3.9 13.9 1.0 CD1 B:TRP304 3.9 14.0 1.0 CE2 B:TRP304 3.9 16.2 1.0 ND1 B:HIS305 4.0 14.1 1.0 CB B:ASP184 4.2 10.3 1.0 O B:HOH554 4.2 8.8 1.0 CB B:ASP151 4.2 12.8 1.0 CZ2 B:TRP304 4.3 14.4 1.0 CD B:ARG130 4.6 13.1 1.0 O B:HOH539 4.7 12.2 1.0 OE1 B:GLU183 4.8 9.8 1.0 CG B:TRP304 4.9 14.3 1.0 CZ3 B:TRP199 4.9 10.2 1.0 CD2 B:TRP304 5.0 14.9 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Tannerella Forsythia Glutaminyl Cyclase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Tannerella Forsythia Glutaminyl Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn401 b:17.8 occ:1.00 OD2 C:ASP184 1.9 14.2 1.0 OD1 C:ASP184 2.0 15.7 1.0 O C:HOH590 2.0 11.1 1.0 OD2 C:ASP151 2.2 12.4 1.0 CG C:ASP184 2.2 11.9 1.0 NE2 C:HIS305 2.3 15.5 1.0 CG C:ASP151 2.9 11.2 1.0 OD1 C:ASP151 3.1 10.5 1.0 CD2 C:HIS305 3.2 13.3 1.0 CE1 C:HIS305 3.3 12.7 1.0 CB C:ASP184 3.7 11.9 1.0 NE1 C:TRP304 3.8 13.4 1.0 CB C:ASP151 4.4 13.6 1.0 OE1 C:GLU183 4.4 18.8 1.0 CG C:HIS305 4.4 13.3 1.0 ND1 C:HIS305 4.4 12.4 1.0 CD C:ARG130 4.5 14.6 1.0 CD1 C:TRP304 4.6 12.3 1.0 CA C:ASP184 4.6 12.8 1.0 O C:HOH554 4.6 7.7 1.0 CE2 C:TRP304 4.7 15.0 1.0 O C:HOH569 4.7 9.4 1.0 NE2 C:HIS126 4.8 8.7 1.0 CB C:ARG130 4.8 14.0 1.0 CE1 C:HIS126 5.0 8.0 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Tannerella Forsythia Glutaminyl Cyclase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Tannerella Forsythia Glutaminyl Cyclase within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn401 b:17.6 occ:1.00 NE2 D:HIS305 1.9 13.8 1.0 OD2 D:ASP151 2.1 13.0 1.0 O D:HOH601 2.2 15.7 1.0 OD2 D:ASP184 2.3 11.2 1.0 OD1 D:ASP184 2.6 13.5 1.0 CD2 D:HIS305 2.6 11.2 1.0 CG D:ASP184 2.8 10.9 1.0 CE1 D:HIS305 3.1 11.3 1.0 CG D:ASP151 3.2 8.6 1.0 NE1 D:TRP304 3.5 11.2 1.0 OD1 D:ASP151 3.7 9.5 1.0 CG D:HIS305 3.9 10.0 1.0 O D:HOH621 3.9 8.0 1.0 ND1 D:HIS305 4.1 12.7 1.0 CD1 D:TRP304 4.2 11.8 1.0 O D:HOH573 4.2 4.5 1.0 O D:HOH541 4.2 5.5 1.0 CD D:ARG130 4.2 11.7 1.0 CB D:ASP184 4.3 10.2 1.0 CB D:ASP151 4.3 10.3 1.0 CE2 D:TRP304 4.4 11.6 1.0 CB D:ARG130 4.6 11.7 1.0 OE2 D:GLU183 4.7 12.6 1.0 CZ2 D:TRP304 4.8 10.1 1.0

N.Taudte, M.Linnert. Identification of A Mammalian Like Type II Glutaminyl Cyclases in the Oral Pathogenic Bacteria P. Gingivalis, T. Forsythia and P. Intermedia To Be Published.