Zinc in PDB 4fke: Crystal Structure of Porcine Aminopeptidase-N

All present enzymatic activity of Crystal Structure of Porcine Aminopeptidase-N:
3.4.11.2;

The structure of Crystal Structure of Porcine Aminopeptidase-N, PDB code: 4fke was solved by L.Chen, Y.L.Lin, G.Peng, F.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.70 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	259.971, 62.770, 81.794, 90.00, 100.12, 90.00
R / Rfree (%)	14.2 / 18.2

The binding sites of Zinc atom in the Crystal Structure of Porcine Aminopeptidase-N (pdb code 4fke). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Porcine Aminopeptidase-N, PDB code: 4fke:

Zinc binding site 1 out of 1 in the Crystal Structure of Porcine Aminopeptidase-N


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 Porcine Aminopeptidase-N within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1024 b:22.2 occ:1.00 OE2 A:GLU406 1.9 18.6 1.0 O A:HOH1526 1.9 21.1 1.0 NE2 A:HIS383 2.1 19.4 1.0 NE2 A:HIS387 2.1 16.3 1.0 CD A:GLU406 2.7 18.2 1.0 OE1 A:GLU406 2.9 20.6 1.0 CD2 A:HIS387 3.0 16.1 1.0 CD2 A:HIS383 3.0 18.2 1.0 CE1 A:HIS383 3.1 17.1 1.0 CE1 A:HIS387 3.2 17.4 1.0 O A:HOH1257 3.8 28.0 1.0 OE2 A:GLU384 4.0 21.5 1.0 OE1 A:GLU350 4.1 17.4 1.0 CB A:ALA409 4.1 17.3 1.0 CG A:HIS383 4.1 16.8 1.0 CG A:HIS387 4.2 15.5 1.0 ND1 A:HIS383 4.2 16.9 1.0 CG A:GLU406 4.2 15.6 1.0 ND1 A:HIS387 4.2 17.8 1.0 O A:HOH1500 4.3 42.6 1.0 O A:HOH1289 4.4 27.0 1.0 CA A:GLU406 4.5 17.6 1.0 OE1 A:GLU384 4.5 20.2 1.0 CE2 A:TYR472 4.5 17.5 1.0 CD A:GLU350 4.6 16.6 1.0 CB A:GLU406 4.6 17.1 1.0 CD A:GLU384 4.6 19.9 1.0 OE2 A:GLU350 4.8 18.5 1.0 OH A:TYR472 5.0 19.9 1.0 O A:HOH1159 5.0 34.9 1.0

L.Chen, Y.L.Lin, G.Peng, F.Li. Structural Basis For Multifunctional Roles of Mammalian Aminopeptidase N. Proc.Natl.Acad.Sci.Usa V. 109 17966 2012.
ISSN: ISSN 0027-8424
PubMed: 23071329
DOI: 10.1073/PNAS.1210123109