Zinc in PDB 1rtq: The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica

All present enzymatic activity of The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica:
3.4.11.10;

The structure of The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica, PDB code: 1rtq was solved by W.Desmarais, D.L.Bienvenue, B.P.Krzysztof, R.C.Holz, G.A.Petsko, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 0.95
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	109.936, 109.936, 91.369, 90.00, 90.00, 120.00
R / Rfree (%)	13.5 / 15.1

The structure of The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica also contains other interesting chemical elements:

Sodium

(Na)

3 atoms

The binding sites of Zinc atom in the The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica (pdb code 1rtq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica, PDB code: 1rtq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:7.0 occ:1.00 O A:HOH1095 2.0 8.6 1.0 NE2 A:HIS256 2.0 7.7 1.0 OD2 A:ASP117 2.0 7.6 1.0 OE2 A:GLU152 2.1 7.4 1.0 O A:HOH1189 2.3 27.6 1.0 OE1 A:GLU152 2.5 7.9 1.0 CD A:GLU152 2.6 7.3 1.0 CG A:ASP117 3.0 5.8 1.0 CE1 A:HIS256 3.0 13.2 1.0 CD2 A:HIS256 3.0 7.4 1.0 HD2 A:HIS256 3.2 8.9 1.0 HE1 A:HIS256 3.2 15.8 1.0 OD1 A:ASP117 3.3 6.6 1.0 ZN A:ZN702 3.3 5.5 1.0 HD13 A:ILE255 3.7 15.4 1.0 O A:HOH1130 3.8 20.7 1.0 O A:HOH1168 4.0 21.2 1.0 HE1 A:HIS97 4.1 7.4 1.0 CG A:GLU152 4.1 7.6 1.0 ND1 A:HIS256 4.1 12.1 1.0 O A:HOH1006 4.2 7.0 1.0 CG A:HIS256 4.2 7.7 1.0 OE1 A:GLU151 4.2 8.4 1.0 HG23 A:THR101 4.2 14.8 1.0 CB A:ASP117 4.3 5.5 1.0 HB3 A:ASP117 4.5 6.6 1.0 HG2 A:GLU152 4.5 9.2 1.0 HG3 A:GLU152 4.5 9.2 1.0 O A:HOH1188 4.5 22.1 1.0 NE2 A:HIS97 4.5 5.7 1.0 CE1 A:HIS97 4.6 6.2 1.0 CD1 A:ILE255 4.7 10.3 1.0 HB2 A:ASP117 4.7 6.6 1.0 HB A:ILE255 4.7 9.1 1.0 HG21 A:THR101 4.8 14.8 1.0 HA A:GLU152 4.8 9.5 1.0 HD1 A:HIS256 4.9 14.5 1.0 CG2 A:THR101 4.9 9.8 1.0 HD12 A:ILE255 5.0 15.4 1.0

Zinc binding site 2 out of 2 in the The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The 0.95 Angstrom Resolution Crystal Structure of the Aminopeptidase From Aeromonas Proteolytica within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:5.5 occ:1.00 O A:HOH1095 1.9 8.6 1.0 OD1 A:ASP117 2.0 6.6 1.0 NE2 A:HIS97 2.0 5.7 1.0 OD1 A:ASP179 2.1 9.2 1.0 OD2 A:ASP179 2.3 10.0 1.0 CG A:ASP179 2.6 8.7 1.0 CE1 A:HIS97 3.0 6.2 1.0 CG A:ASP117 3.0 5.8 1.0 CD2 A:HIS97 3.1 5.3 1.0 HE1 A:HIS97 3.1 7.4 1.0 HB2 A:ASP118 3.2 6.3 1.0 O A:HOH1168 3.2 21.2 1.0 HD2 A:HIS97 3.3 6.4 1.0 ZN A:ZN701 3.3 7.0 1.0 OD2 A:ASP117 3.4 7.6 1.0 OE2 A:GLU152 3.7 7.4 1.0 OE1 A:GLU151 3.7 8.4 1.0 HA A:ASP117 4.1 6.3 1.0 CD A:GLU151 4.1 8.6 1.0 HG3 A:MET180 4.1 7.5 1.0 CB A:ASP179 4.1 8.1 1.0 CB A:ASP118 4.1 5.2 1.0 ND1 A:HIS97 4.1 5.9 1.0 CG A:HIS97 4.2 5.4 1.0 OE2 A:GLU151 4.3 17.4 1.0 CB A:ASP117 4.3 5.5 1.0 O A:HOH1189 4.4 27.6 1.0 CD A:GLU152 4.4 7.3 1.0 HB2 A:ASP179 4.5 9.7 1.0 HB3 A:ASP118 4.5 6.3 1.0 CA A:ASP117 4.5 5.2 1.0 HA A:ASP179 4.5 7.6 1.0 O A:HOH1130 4.6 20.7 1.0 HB3 A:ASP179 4.6 9.7 1.0 HB2 A:ASP117 4.6 6.6 1.0 OE1 A:GLU152 4.6 7.9 1.0 C A:ASP117 4.7 5.2 1.0 CG A:ASP118 4.7 5.1 1.0 OG A:SER228 4.8 7.9 1.0 CA A:ASP179 4.8 6.3 1.0 N A:ASP118 4.8 5.0 1.0 HD1 A:HIS97 4.9 7.1 1.0 CG A:MET180 4.9 6.3 1.0 CA A:ASP118 4.9 4.8 1.0 OD2 A:ASP118 5.0 5.5 1.0 HA A:ASP118 5.0 5.7 1.0 HB3 A:ASP117 5.0 6.6 1.0 HG3 A:GLU151 5.0 8.2 1.0

W.Desmarais, D.L.Bienvenue, K.P.Bzymek, G.A.Petsko, D.Ringe, R.C.Holz. The High-Resolution Structures of the Neutral and the Low pH Crystals of Aminopeptidase From Aeromonas Proteolytica. J.Biol.Inorg.Chem. V. 11 398 2006.
ISSN: ISSN 0949-8257
PubMed: 16596389
DOI: 10.1007/S00775-006-0093-X