Zinc in PDB 2anp: Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica.

All present enzymatic activity of Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica.:
3.4.11.10;

The structure of Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica., PDB code: 2anp was solved by K.P.Bzymek, A.Moulin, S.I.Swierczek, D.Ringe, G.A.Petsko, R.C.Holz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	109.090, 109.090, 98.417, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 20.5

The structure of Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica. also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Zinc atom in the Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica. (pdb code 2anp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica., PDB code: 2anp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Functional Glutamate 151 to Histidine Mutant 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 Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:16.6 occ:1.00 O A:HOH587 2.0 11.2 1.0 OE2 A:GLU152 2.0 13.1 1.0 OD2 A:ASP117 2.0 14.8 1.0 NE2 A:HIS256 2.1 20.5 1.0 OE1 A:GLU152 2.6 15.9 1.0 CD A:GLU152 2.6 15.2 1.0 CG A:ASP117 3.0 15.2 1.0 CD2 A:HIS256 3.0 19.5 1.0 CE1 A:HIS256 3.1 22.3 1.0 OD1 A:ASP117 3.2 12.8 1.0 ZN A:ZN502 3.3 15.0 1.0 O A:HOH521 3.9 14.5 1.0 CG A:GLU152 4.1 15.2 1.0 ND1 A:HIS256 4.2 22.0 1.0 CG A:HIS256 4.2 20.9 1.0 CB A:ASP117 4.3 10.8 1.0 CE1 A:HIS97 4.4 11.0 1.0 NE2 A:HIS97 4.4 10.1 1.0 NE2 A:HIS151 4.4 15.3 1.0 CD2 A:HIS151 4.5 13.7 1.0 CG2 A:THR101 4.9 16.6 1.0 CD1 A:ILE255 5.0 18.3 1.0 O A:HOH573 5.0 47.0 1.0

Zinc binding site 2 out of 2 in the Functional Glutamate 151 to Histidine Mutant 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 Functional Glutamate 151 to Histidine Mutant of the Aminopeptidase From Aeromonas Proteolytica. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:15.0 occ:1.00 OD1 A:ASP117 1.9 12.8 1.0 OD1 A:ASP179 2.1 12.6 1.0 O A:HOH587 2.1 11.2 1.0 NE2 A:HIS97 2.1 10.1 1.0 OD2 A:ASP179 2.6 13.0 1.0 CG A:ASP179 2.7 12.3 1.0 CG A:ASP117 3.0 15.2 1.0 CE1 A:HIS97 3.1 11.0 1.0 CD2 A:HIS97 3.2 11.4 1.0 ZN A:ZN501 3.3 16.6 1.0 OD2 A:ASP117 3.4 14.8 1.0 NE2 A:HIS151 3.7 15.3 1.0 OE2 A:GLU152 4.0 13.1 1.0 CB A:ASP118 4.1 11.0 1.0 CD2 A:HIS151 4.1 13.7 1.0 CE1 A:HIS151 4.1 16.4 1.0 CB A:ASP179 4.2 11.7 1.0 ND1 A:HIS97 4.2 12.0 1.0 CB A:ASP117 4.3 10.8 1.0 CG A:HIS97 4.3 11.0 1.0 CA A:ASP117 4.6 12.2 1.0 CG A:ASP118 4.7 12.6 1.0 CD A:GLU152 4.7 15.2 1.0 CG A:MET180 4.7 12.1 1.0 ND1 A:HIS151 4.8 14.5 1.0 CG A:HIS151 4.8 14.8 1.0 CA A:ASP179 4.8 11.2 1.0 C A:ASP117 4.8 11.5 1.0 SD A:MET180 4.8 16.4 1.0 OE1 A:GLU152 4.9 15.9 1.0 OD1 A:ASP118 4.9 11.4 1.0 N A:ASP118 4.9 10.5 1.0 CA A:ASP118 4.9 12.0 1.0

K.P.Bzymek, A.Moulin, S.I.Swierczek, D.Ringe, G.A.Petsko, B.Bennett, R.C.Holz. Kinetic, Spectroscopic, and X-Ray Crystallographic Characterization of the Functional E151H Aminopeptidase From Aeromonas Proteolytica. Biochemistry V. 44 12030 2005.
ISSN: ISSN 0006-2960
PubMed: 16142900
DOI: 10.1021/BI0505823