Zinc in PDB 1amp: Crystal Structure of Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family

All present enzymatic activity of Crystal Structure of Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family:
3.4.11.10;

The structure of Crystal Structure of Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family, PDB code: 1amp was solved by B.Chevrier, C.Schalk, H.D'orchymont, J.M.Rondeau, D.Moras, C.Tarnus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.80
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	111.000, 111.000, 92.100, 90.00, 90.00, 120.00
R / Rfree (%)	16.1 / n/a

The binding sites of Zinc atom in the Crystal Structure of Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family (pdb code 1amp). 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 Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family, PDB code: 1amp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family


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 Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:12.8 occ:1.00 OE2 A:GLU152 2.0 9.3 1.0 OD2 A:ASP117 2.0 6.7 1.0 O A:HOH935 2.2 24.1 1.0 NE2 A:HIS256 2.3 14.1 1.0 OE1 A:GLU152 2.4 10.4 1.0 CD A:GLU152 2.5 10.4 1.0 CG A:ASP117 3.0 7.1 1.0 CD2 A:HIS256 3.0 14.0 1.0 OD1 A:ASP117 3.3 7.1 1.0 CE1 A:HIS256 3.4 14.6 1.0 ZN A:ZN502 3.5 10.4 1.0 O A:HOH604 3.7 9.4 1.0 O A:HOH919 3.8 28.5 1.0 CG A:GLU152 4.1 8.4 1.0 O A:HOH937 4.1 37.4 1.0 O A:HOH699 4.1 31.6 1.0 OE1 A:GLU151 4.1 8.0 1.0 CG A:HIS256 4.2 13.1 1.0 ND1 A:HIS256 4.3 15.8 1.0 CB A:ASP117 4.4 4.3 1.0 CE1 A:HIS97 4.5 6.1 1.0 NE2 A:HIS97 4.5 5.6 1.0 O A:HOH934 4.6 44.8 1.0 CG2 A:THR101 4.7 9.9 1.0 CD1 A:ILE255 4.7 13.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family


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 Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:10.4 occ:1.00 OD1 A:ASP117 2.0 7.1 1.0 OD1 A:ASP179 2.1 10.6 1.0 NE2 A:HIS97 2.2 5.6 1.0 O A:HOH935 2.3 24.1 1.0 OD2 A:ASP179 2.3 10.3 1.0 CG A:ASP179 2.5 9.1 1.0 CG A:ASP117 3.1 7.1 1.0 O A:HOH934 3.1 44.8 1.0 CE1 A:HIS97 3.2 6.1 1.0 CD2 A:HIS97 3.2 5.5 1.0 OD2 A:ASP117 3.4 6.7 1.0 ZN A:ZN501 3.5 12.8 1.0 OE1 A:GLU151 3.8 8.0 1.0 OE2 A:GLU152 4.0 9.3 1.0 CB A:ASP179 4.1 8.7 1.0 CB A:ASP118 4.2 4.1 1.0 CD A:GLU151 4.2 10.7 1.0 ND1 A:HIS97 4.3 8.7 1.0 CG A:HIS97 4.3 5.5 1.0 CB A:ASP117 4.4 4.3 1.0 OE2 A:GLU151 4.4 13.4 1.0 O A:HOH937 4.6 37.4 1.0 CD A:GLU152 4.6 10.4 1.0 O A:HOH919 4.6 28.5 1.0 CA A:ASP117 4.7 6.9 1.0 CG A:ASP118 4.7 4.2 1.0 OE1 A:GLU152 4.7 10.4 1.0 CG A:MET180 4.8 3.9 1.0 N A:ASP118 4.8 5.8 1.0 SD A:MET180 4.8 10.4 1.0 CA A:ASP179 4.8 7.6 1.0 OG A:SER228 4.8 7.4 1.0 OD2 A:ASP118 4.9 6.8 1.0 C A:ASP117 5.0 6.2 1.0

B.Chevrier, C.Schalk, H.D'orchymont, J.M.Rondeau, D.Moras, C.Tarnus. Crystal Structure of Aeromonas Proteolytica Aminopeptidase: A Prototypical Member of the Co-Catalytic Zinc Enzyme Family. Structure V. 2 283 1994.
ISSN: ISSN 0969-2126
PubMed: 8087555
DOI: 10.1016/S0969-2126(00)00030-7