Zinc in PDB 1fno: Peptidase T (Tripeptidase)

The structure of Peptidase T (Tripeptidase), PDB code: 1fno was solved by K.Hakansson, C.G.Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	500.00 / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	132.374, 46.036, 96.591, 90.00, 116.11, 90.00
R / Rfree (%)	22.2 / 26.1

The binding sites of Zinc atom in the Peptidase T (Tripeptidase) (pdb code 1fno). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Peptidase T (Tripeptidase), PDB code: 1fno:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Peptidase T (Tripeptidase)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Peptidase T (Tripeptidase) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:36.9 occ:1.00 OD2 A:ASP140 2.0 26.5 1.0 OD1 A:ASP196 2.2 28.8 1.0 NE2 A:HIS78 2.2 21.9 1.0 OD2 A:ASP196 2.5 28.8 1.0 CG A:ASP196 2.7 28.8 1.0 CG A:ASP140 3.0 26.5 1.0 CD2 A:HIS78 3.1 21.9 1.0 CE1 A:HIS78 3.3 21.9 1.0 ZN A:ZN502 3.4 0.8 1.0 OD1 A:ASP140 3.4 26.5 1.0 CB A:ASP141 3.8 20.8 1.0 OE1 A:GLU173 3.9 39.7 1.0 CB A:ASP196 4.2 28.8 1.0 OE1 A:GLU174 4.2 52.4 1.0 CG A:HIS78 4.3 21.9 1.0 CG A:ASP141 4.3 20.8 1.0 ND1 A:HIS78 4.3 21.9 1.0 CB A:ASP140 4.3 26.5 1.0 CD A:GLU173 4.5 39.7 1.0 O A:ASP196 4.5 37.9 1.0 OD1 A:ASP141 4.6 20.8 1.0 O A:HOH664 4.6 64.4 1.0 CA A:ASP141 4.6 28.8 1.0 N A:ASP141 4.7 28.8 1.0 C A:ASP140 4.7 26.8 1.0 CA A:ASP140 4.7 26.8 1.0 OD2 A:ASP141 4.9 20.8 1.0 CA A:ASP196 4.9 37.9 1.0 CD A:GLU174 5.0 52.4 1.0

Zinc binding site 2 out of 2 in the Peptidase T (Tripeptidase)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Peptidase T (Tripeptidase) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:0.8 occ:1.00 OD1 A:ASP140 2.3 26.5 1.0 OE1 A:GLU174 2.5 52.4 1.0 NE2 A:HIS379 2.7 68.3 1.0 O A:HOH664 3.1 64.4 1.0 OE2 A:GLU174 3.2 52.4 1.0 CG A:ASP140 3.2 26.5 1.0 CD A:GLU174 3.2 52.4 1.0 ZN A:ZN501 3.4 36.9 1.0 OD2 A:ASP140 3.4 26.5 1.0 CE1 A:HIS379 3.5 68.3 1.0 CD2 A:HIS379 3.7 68.3 1.0 OE1 A:GLU173 4.2 39.7 1.0 CB A:ASP140 4.6 26.5 1.0 NE2 A:HIS78 4.6 21.9 1.0 ND1 A:HIS379 4.6 68.3 1.0 CG A:GLU174 4.7 52.4 1.0 CG A:HIS379 4.8 68.3 1.0 CE1 A:HIS78 4.9 21.9 1.0 CB A:TYR378 5.0 38.5 1.0

K.Hakansson, C.G.Miller. Structure of Peptidase T From Salmonella Typhimurium Eur.J.Biochem. V. 269 443 2002.
ISSN: ISSN 0014-2956
PubMed: 11856302
DOI: 10.1046/J.0014-2956.2001.02665.X