Zinc in PDB 2iq6: Crystal Structure of the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine.

All present enzymatic activity of Crystal Structure of the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine.:
3.4.11.10;

The structure of Crystal Structure of the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine., PDB code: 2iq6 was solved by A.Kumar, B.Narayanan, J.-J.P.Kim, B.Bennett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	108.400, 108.400, 96.800, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 24.7

The binding sites of Zinc atom in the Crystal Structure of the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine. (pdb code 2iq6). 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 the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine., PDB code: 2iq6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine.


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 the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn292 b:28.5 occ:1.00 NE2 A:HIS256 2.2 31.3 1.0 OE2 A:GLU152 2.2 22.6 1.0 OD2 A:ASP117 2.2 25.2 1.0 O B:LEU294 2.3 24.0 1.0 OE1 A:GLU152 2.4 19.1 1.0 CD A:GLU152 2.6 19.3 1.0 CG A:ASP117 3.0 27.6 1.0 C B:LEU294 3.0 24.0 1.0 OD1 A:ASP117 3.1 20.4 1.0 CE1 A:HIS256 3.2 34.8 1.0 CD2 A:HIS256 3.2 32.2 1.0 ZN A:ZN293 3.4 22.4 1.0 N B:LEU294 3.7 24.0 1.0 N B:LEU296 3.9 23.8 1.0 N B:LEU295 3.9 24.0 1.0 CD2 B:LEU295 3.9 24.0 1.0 CA B:LEU294 3.9 24.0 1.0 O A:HOH304 3.9 20.5 1.0 CG A:GLU152 4.1 21.5 1.0 C B:LEU295 4.2 24.0 1.0 ND1 A:HIS256 4.3 34.3 1.0 CG A:HIS256 4.3 32.4 1.0 CB A:ASP117 4.3 29.9 1.0 OE1 A:GLU151 4.4 21.5 1.0 NE2 A:HIS97 4.6 20.2 1.0 CB B:LEU294 4.6 24.0 1.0 CA B:LEU295 4.7 24.0 1.0 CE1 A:HIS97 4.8 18.9 1.0 CG2 A:THR101 4.8 28.2 1.0 CA B:LEU296 5.0 23.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine.


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 the Aminopeptidase From Vibrio Proteolyticus in Complexation with Leucyl-Leucyl-Leucine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn293 b:22.4 occ:1.00 O B:LEU294 1.9 24.0 1.0 OD1 A:ASP117 2.1 20.4 1.0 OD1 A:ASP179 2.2 21.7 1.0 NE2 A:HIS97 2.3 20.2 1.0 OD2 A:ASP179 2.5 21.9 1.0 N B:LEU294 2.5 24.0 1.0 CG A:ASP179 2.7 22.7 1.0 C B:LEU294 2.7 24.0 1.0 CA B:LEU294 2.9 24.0 1.0 OD2 A:ASP118 3.0 43.0 1.0 CG A:ASP117 3.1 27.6 1.0 CD2 A:HIS97 3.2 18.6 1.0 CE1 A:HIS97 3.3 18.9 1.0 ZN A:ZN292 3.4 28.5 1.0 OD2 A:ASP117 3.5 25.2 1.0 OE1 A:GLU151 3.8 21.5 1.0 OE2 A:GLU152 3.9 22.6 1.0 N B:LEU295 3.9 24.0 1.0 CG A:ASP118 4.0 34.8 1.0 CB A:ASP179 4.2 20.8 1.0 CD A:GLU151 4.3 23.1 1.0 ND1 A:HIS97 4.4 18.8 1.0 CB A:ASP118 4.4 32.3 1.0 CG A:HIS97 4.4 20.6 1.0 CD A:GLU152 4.4 19.3 1.0 CB A:ASP117 4.4 29.9 1.0 CB B:LEU294 4.4 24.0 1.0 C A:ASP117 4.5 34.2 1.0 CA A:ASP117 4.6 30.2 1.0 OE1 A:GLU152 4.6 19.1 1.0 N A:ASP118 4.6 35.1 1.0 OE2 A:GLU151 4.6 26.6 1.0 CG A:MET180 4.7 18.6 1.0 O A:ASP117 4.8 34.8 1.0 CA A:ASP179 4.8 20.6 1.0 OG A:SER228 4.9 18.9 1.0 SD A:MET180 4.9 22.2 1.0

A.Kumar, G.R.Periyannan, B.Narayanan, A.W.Kittell, J.-J.Kim, B.Bennett. Experimental Evidence For A Metallohydrolase Mechanism in Which the Nucleophile Is Not Delivered By A Metal Ion: Epr Spectrokinetic and Structural Studies of Aminopeptidase From Vibrio Proteolyticus Biochem.J. V. 403 527 2007.
ISSN: ISSN 0264-6021
PubMed: 17238863
DOI: 10.1042/BJ20061591