Zinc in PDB 1txr: X-Ray Crystal Structure of Bestatin Bound to Aap

All present enzymatic activity of X-Ray Crystal Structure of Bestatin Bound to Aap:
3.4.11.10;

The structure of X-Ray Crystal Structure of Bestatin Bound to Aap, PDB code: 1txr was solved by C.C.Stamper, R.C.Holz, D.Ringe, G.A.Petsko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	107.800, 107.800, 102.600, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 24.5

The binding sites of Zinc atom in the X-Ray Crystal Structure of Bestatin Bound to Aap (pdb code 1txr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Crystal Structure of Bestatin Bound to Aap, PDB code: 1txr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the X-Ray Crystal Structure of Bestatin Bound to Aap


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Crystal Structure of Bestatin Bound to Aap within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:13.0 occ:1.00 OD2 A:ASP117 2.0 8.2 1.0 O2 A:BES503 2.1 9.7 1.0 NE2 A:HIS256 2.1 14.6 1.0 OE2 A:GLU152 2.1 10.1 1.0 O3 A:BES503 2.3 15.7 1.0 OE1 A:GLU152 2.3 8.3 1.0 CD A:GLU152 2.5 6.2 1.0 C2 A:BES503 2.9 12.7 1.0 CE1 A:HIS256 2.9 17.3 1.0 C3 A:BES503 2.9 15.0 1.0 CG A:ASP117 3.1 11.7 1.0 CD2 A:HIS256 3.2 13.8 1.0 OD1 A:ASP117 3.5 13.6 1.0 ZN A:ZN502 3.5 13.5 1.0 C1 A:BES503 3.5 12.5 1.0 CG A:GLU152 4.0 7.8 1.0 ND1 A:HIS256 4.1 17.1 1.0 O A:HOH556 4.1 15.8 1.0 OE1 A:GLU151 4.1 10.7 1.0 N1 A:BES503 4.3 14.6 1.0 CG A:HIS256 4.3 13.1 1.0 N2 A:BES503 4.3 11.3 1.0 CB A:ASP117 4.4 9.8 1.0 O A:HOH517 4.4 13.0 1.0 NE2 A:HIS97 4.6 10.5 1.0 CE1 A:HIS97 4.6 10.2 1.0 CG2 A:THR101 4.8 13.1 1.0 CD1 A:ILE255 4.8 11.4 1.0 C6 A:BES503 4.9 16.3 1.0 CB A:GLU152 4.9 9.1 1.0

Zinc binding site 2 out of 2 in the X-Ray Crystal Structure of Bestatin Bound to Aap


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of X-Ray Crystal Structure of Bestatin Bound to Aap within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:13.5 occ:1.00 O2 A:BES503 1.9 9.7 1.0 OD1 A:ASP117 2.0 13.6 1.0 OD1 A:ASP179 2.2 11.6 1.0 NE2 A:HIS97 2.2 10.5 1.0 N2 A:BES503 2.3 11.3 1.0 OD2 A:ASP179 2.4 11.8 1.0 CG A:ASP179 2.6 11.3 1.0 C2 A:BES503 2.7 12.7 1.0 CG A:ASP117 2.9 11.7 1.0 C1 A:BES503 2.9 12.5 1.0 CE1 A:HIS97 3.2 10.2 1.0 OD2 A:ASP117 3.2 8.2 1.0 CD2 A:HIS97 3.2 5.6 1.0 ZN A:ZN501 3.5 13.0 1.0 OE2 A:GLU152 3.9 10.1 1.0 OE1 A:GLU151 3.9 10.7 1.0 CB A:ASP179 4.1 10.6 1.0 CB A:ASP118 4.1 6.8 1.0 C3 A:BES503 4.1 15.0 1.0 CB A:ASP117 4.2 9.8 1.0 ND1 A:HIS97 4.3 9.2 1.0 C6 A:BES503 4.3 16.3 1.0 CG A:HIS97 4.3 9.7 1.0 CD A:GLU151 4.4 10.7 1.0 OE2 A:GLU151 4.5 10.7 1.0 CA A:ASP117 4.6 8.8 1.0 O3 A:BES503 4.6 15.7 1.0 CD A:GLU152 4.7 6.2 1.0 CG A:ASP118 4.7 9.9 1.0 OG A:SER228 4.8 8.1 1.0 CA A:ASP179 4.8 10.8 1.0 SD A:MET180 4.8 12.0 1.0 C A:ASP117 4.8 8.2 1.0 CG A:MET180 4.9 5.2 1.0 CA A:ASP118 5.0 9.1 1.0 OE1 A:GLU152 5.0 8.3 1.0 N A:ASP118 5.0 8.0 1.0

C.C.Stamper, D.L.Bienvenue, B.Bennett, D.Ringe, G.A.Petsko, R.C.Holz. Spectroscopic and X-Ray Crystallographic Characterization of Bestatin Bound to the Aminopeptidase From Aeromonas (Vibrio) Proteolytica. Biochemistry V. 43 9620 2004.
ISSN: ISSN 0006-2960
PubMed: 15274616
DOI: 10.1021/BI049126P