Zinc in PDB 2ewb: The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat

All present enzymatic activity of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat:
3.4.11.1;

The structure of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat, PDB code: 2ewb was solved by V.Alterio, C.Pedone, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.85
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	128.940, 128.940, 119.790, 90.00, 90.00, 120.00
R / Rfree (%)	15.6 / 17.7

The structure of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Zinc atom in the The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat (pdb code 2ewb). 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 Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat, PDB code: 2ewb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn488 b:9.8 occ:1.00 OD1 A:ASP332 2.0 7.8 1.0 OE1 A:GLU334 2.0 7.4 1.0 OD2 A:ASP255 2.0 6.4 1.0 O A:ASP332 2.1 7.3 1.0 SZ2 A:ZED2000 2.3 12.0 1.0 CD A:GLU334 2.9 9.7 1.0 CG A:ASP255 3.0 7.7 1.0 CG A:ASP332 3.0 9.9 1.0 C A:ASP332 3.0 9.1 1.0 ZN A:ZN489 3.1 9.0 1.0 OE2 A:GLU334 3.2 7.2 1.0 OD1 A:ASP255 3.3 8.7 1.0 CA A:ASP332 3.4 9.5 1.0 CZF A:ZED2000 3.4 13.7 1.0 CB A:ASP332 3.8 8.3 1.0 NZ A:LYS262 3.9 11.1 1.0 OD2 A:ASP332 3.9 8.9 1.0 CE A:LYS262 3.9 10.5 1.0 OZ3 A:ZED2000 4.1 15.9 1.0 CZE A:ZED2000 4.2 15.7 1.0 N A:ALA333 4.2 6.3 1.0 N A:GLU334 4.3 6.5 1.0 CG A:GLU334 4.3 8.2 1.0 CB A:ASP255 4.3 7.1 1.0 ND2 A:ASN305 4.4 7.3 1.0 CZD A:ZED2000 4.4 14.1 1.0 OD2 A:ASP273 4.5 9.0 1.0 O2 A:CO3500 4.6 9.2 1.0 CA A:GLY257 4.6 8.0 1.0 NZ1 A:ZED2000 4.6 17.1 1.0 CA A:ALA333 4.7 7.8 1.0 N A:ASP332 4.8 7.9 1.0 NZ A:LYS250 4.8 5.6 1.0 CB A:GLU334 4.9 7.1 1.0 O A:THR331 4.9 8.5 1.0

Zinc binding site 2 out of 2 in the The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of Bovine Lens Leucine Aminopeptidase in Complex with Zofenoprilat within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn489 b:9.0 occ:1.00 OD2 A:ASP273 2.0 9.0 1.0 OE2 A:GLU334 2.0 7.2 1.0 NZ A:LYS250 2.1 5.6 1.0 SZ2 A:ZED2000 2.3 12.0 1.0 CG A:ASP273 2.7 8.8 1.0 CE A:LYS250 2.8 5.9 1.0 OD2 A:ASP255 2.8 6.4 1.0 OD1 A:ASP273 2.9 9.7 1.0 CD A:GLU334 3.1 9.7 1.0 ZN A:ZN488 3.1 9.8 1.0 CZF A:ZED2000 3.3 13.7 1.0 OE1 A:GLU334 3.4 7.4 1.0 CG A:ASP255 3.7 7.7 1.0 O2 A:CO3500 3.8 9.2 1.0 CB A:ASP255 4.1 7.1 1.0 CE A:MET270 4.1 15.4 1.0 CB A:ASP273 4.2 7.1 1.0 O A:THR359 4.3 9.6 1.0 CD A:LYS250 4.3 5.7 1.0 CG A:GLU334 4.4 8.2 1.0 CG1 A:ILE252 4.5 6.2 1.0 N A:GLY335 4.5 7.9 1.0 O A:ASP332 4.6 7.3 1.0 OD1 A:ASP255 4.6 8.7 1.0 CB A:ILE252 4.7 7.5 1.0 CZD A:ZED2000 4.7 14.1 1.0 CG2 A:ILE252 4.8 6.9 1.0 CA A:GLY335 4.9 8.3 1.0 OD1 A:ASP332 5.0 7.8 1.0 C A:CO3500 5.0 9.3 1.0

M.Cappiello, V.Alterio, P.Amodeo, A.Del Corso, A.Scaloni, C.Pedone, R.Moschini, G.M.De Donatis, G.De Simone, U.Mura. Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase. Biochemistry V. 45 3226 2006.
ISSN: ISSN 0006-2960
PubMed: 16519517
DOI: 10.1021/BI052069V