Zinc in PDB 5lg6: Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain

All present enzymatic activity of Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain:
3.4.11.2;

The structure of Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain, PDB code: 5lg6 was solved by C.Santiago, J.Reguera, G.Mudgal, J.M.Casasnovas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.98 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	66.465, 215.690, 78.630, 90.00, 91.90, 90.00
R / Rfree (%)	19.1 / 22.9

The binding sites of Zinc atom in the Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain (pdb code 5lg6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain, PDB code: 5lg6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1010 b:17.2 occ:1.00 NE2 A:HIS383 2.1 7.2 1.0 OE1 A:GLU406 2.1 19.6 1.0 NE2 A:HIS387 2.2 9.2 1.0 O A:HOH1299 2.4 12.7 1.0 CD A:GLU406 2.9 17.9 1.0 CE1 A:HIS383 3.0 8.8 1.0 OE2 A:GLU406 3.0 18.9 1.0 CD2 A:HIS387 3.0 7.2 1.0 CD2 A:HIS383 3.2 5.4 1.0 CE1 A:HIS387 3.3 13.2 1.0 O A:HOH1195 3.4 19.9 1.0 CE2 A:TYR472 3.9 15.1 1.0 OH A:TYR472 3.9 20.1 1.0 ND1 A:HIS383 4.1 9.8 1.0 CG A:HIS387 4.2 7.9 1.0 CG A:HIS383 4.3 5.4 1.0 CZ A:TYR472 4.3 19.8 1.0 ND1 A:HIS387 4.3 14.9 1.0 CG A:GLU406 4.3 12.7 1.0 CB A:ALA409 4.5 8.8 1.0 OE2 A:GLU384 4.7 14.1 1.0 CA A:GLU406 4.8 10.7 1.0 OE1 A:GLU350 4.8 29.3 1.0 CB A:GLU406 4.8 11.0 1.0 CD2 A:TYR472 4.9 18.7 1.0 OE2 A:GLU350 4.9 22.7 1.0

Zinc binding site 2 out of 2 in the Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Deglycosylated Porcine Aminopeptidase N Ectodomain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1010 b:18.9 occ:1.00 OE1 B:GLU406 2.1 19.4 1.0 NE2 B:HIS383 2.2 6.6 1.0 NE2 B:HIS387 2.2 9.5 1.0 CD B:GLU406 2.8 19.9 1.0 OE2 B:GLU406 2.9 19.9 1.0 CD2 B:HIS387 3.0 8.0 1.0 CE1 B:HIS383 3.0 8.8 1.0 CD2 B:HIS383 3.2 5.8 1.0 CE1 B:HIS387 3.3 14.4 1.0 OH B:TYR472 3.9 18.7 1.0 CE2 B:TYR472 3.9 15.6 1.0 CG B:HIS387 4.2 8.1 1.0 ND1 B:HIS383 4.2 11.1 1.0 CG B:GLU406 4.3 13.2 1.0 CZ B:TYR472 4.3 21.6 1.0 ND1 B:HIS387 4.3 13.3 1.0 CG B:HIS383 4.3 5.9 1.0 CB B:ALA409 4.6 10.2 1.0 OE1 B:GLU350 4.7 30.0 1.0 OE2 B:GLU384 4.7 14.9 1.0 CA B:GLU406 4.8 12.5 1.0 CB B:GLU406 4.8 11.3 1.0 OE2 B:GLU350 4.9 25.2 1.0 CD2 B:TYR472 4.9 20.8 1.0

C.Santiago, G.Mudgal, J.Reguera, R.Recacha, S.Albrecht, L.Enjuanes, J.M.Casasnovas. Allosteric Inhibition of Aminopeptidase N Functions Related to Tumor Growth and Virus Infection. Sci Rep V. 7 46045 2017.
ISSN: ESSN 2045-2322
PubMed: 28393915
DOI: 10.1038/SREP46045