Zinc in PDB 1lan: Leucine Aminopeptidase Complex with L-Leucinal

All present enzymatic activity of Leucine Aminopeptidase Complex with L-Leucinal:
3.4.11.1;

The structure of Leucine Aminopeptidase Complex with L-Leucinal, PDB code: 1lan was solved by N.Straeter, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.90
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	131.200, 131.200, 120.900, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 21.2

The binding sites of Zinc atom in the Leucine Aminopeptidase Complex with L-Leucinal (pdb code 1lan). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Leucine Aminopeptidase Complex with L-Leucinal, PDB code: 1lan:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Leucine Aminopeptidase Complex with L-Leucinal


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Leucine Aminopeptidase Complex with L-Leucinal within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn488 b:11.7 occ:1.00 OD1 A:ASP332 2.0 10.1 1.0 OE1 A:GLU334 2.0 7.6 1.0 OD2 A:ASP255 2.1 9.7 1.0 OXT A:LEU500 2.1 25.8 1.0 O A:LEU500 2.2 18.0 1.0 O A:ASP332 2.2 8.5 1.0 C A:LEU500 2.7 24.0 1.0 CD A:GLU334 2.9 10.5 1.0 CG A:ASP332 3.0 10.6 1.0 CG A:ASP255 3.0 9.8 1.0 C A:ASP332 3.1 9.0 1.0 ZN A:ZN489 3.1 14.2 1.0 OE2 A:GLU334 3.2 9.5 1.0 OD1 A:ASP255 3.3 8.3 1.0 CA A:ASP332 3.5 9.7 1.0 CB A:ASP332 3.8 8.4 1.0 N A:LEU500 3.8 23.4 1.0 CA A:LEU500 3.9 24.2 1.0 OD2 A:ASP332 3.9 8.8 1.0 NZ A:LYS262 3.9 8.9 1.0 O A:HOH834 4.1 13.3 1.0 CE A:LYS262 4.2 7.5 1.0 N A:ALA333 4.3 8.2 1.0 N A:GLU334 4.3 8.6 1.0 CG A:GLU334 4.4 8.7 1.0 CB A:ASP255 4.4 8.8 1.0 OD1 A:ASN305 4.5 12.4 1.0 O A:HOH773 4.6 30.2 1.0 OD2 A:ASP273 4.7 13.1 1.0 CA A:ALA333 4.7 8.8 1.0 CB A:LEU500 4.8 24.4 1.0 N A:ASP332 4.9 10.2 1.0 CA A:GLY257 4.9 8.5 1.0 CB A:GLU334 4.9 9.8 1.0 NZ A:LYS250 5.0 10.3 1.0

Zinc binding site 2 out of 3 in the Leucine Aminopeptidase Complex with L-Leucinal


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Leucine Aminopeptidase Complex with L-Leucinal within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn489 b:14.2 occ:1.00 OD2 A:ASP273 2.0 13.1 1.0 O A:LEU500 2.1 18.0 1.0 OE2 A:GLU334 2.1 9.5 1.0 NZ A:LYS250 2.2 10.3 1.0 N A:LEU500 2.4 23.4 1.0 OD2 A:ASP255 2.8 9.7 1.0 CG A:ASP273 2.9 12.0 1.0 OD1 A:ASP273 3.0 10.8 1.0 C A:LEU500 3.0 24.0 1.0 CA A:LEU500 3.1 24.2 1.0 CE A:LYS250 3.1 6.2 1.0 CD A:GLU334 3.1 10.5 1.0 ZN A:ZN488 3.1 11.7 1.0 OE1 A:GLU334 3.5 7.6 1.0 CG A:ASP255 3.5 9.8 1.0 O A:HOH834 3.6 13.3 1.0 OXT A:LEU500 3.6 25.8 1.0 CB A:ASP255 4.0 8.8 1.0 CB A:ASP273 4.3 8.8 1.0 O A:THR359 4.3 9.7 1.0 OD1 A:ASP255 4.5 8.3 1.0 CG A:GLU334 4.5 8.7 1.0 CB A:LEU500 4.5 24.4 1.0 CD A:LYS250 4.5 7.2 1.0 CG1 A:ILE252 4.7 8.1 1.0 O A:ASP332 4.7 8.5 1.0 CB A:ILE252 4.8 9.6 1.0 N A:GLY335 4.8 9.1 1.0 CG2 A:ILE252 4.8 9.4 1.0 OD1 A:ASP332 4.9 10.1 1.0

Zinc binding site 3 out of 3 in the Leucine Aminopeptidase Complex with L-Leucinal


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Leucine Aminopeptidase Complex with L-Leucinal within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn490 b:35.2 occ:1.00 O A:THR173 2.7 12.1 1.0 O A:LEU170 2.8 8.3 1.0 O A:ARG271 2.8 9.8 1.0 O A:HOH562 2.9 7.2 1.0 O A:MET171 2.9 8.2 1.0 C A:MET171 3.5 8.8 1.0 SD A:MET274 3.5 8.6 1.0 C A:ARG271 3.7 8.8 1.0 C A:THR173 3.8 12.6 1.0 CA A:MET171 3.8 8.4 1.0 CG A:MET178 3.8 9.6 1.0 CB A:MET178 3.8 11.0 1.0 C A:LEU170 3.9 9.6 1.0 N A:THR173 4.1 9.3 1.0 CB A:ARG271 4.2 8.7 1.0 CA A:THR173 4.3 10.9 1.0 CG A:MET274 4.3 9.3 1.0 CG A:ARG271 4.3 7.5 1.0 N A:MET171 4.3 8.4 1.0 CE A:MET274 4.3 5.4 1.0 N A:GLU172 4.4 7.6 1.0 C A:GLU172 4.4 9.1 1.0 CB A:THR173 4.5 11.0 1.0 CA A:ARG271 4.5 9.6 1.0 N A:ALA272 4.6 8.2 1.0 CA A:ALA272 4.7 9.1 1.0 CD A:ARG271 4.8 9.2 1.0 O A:GLU172 4.9 10.3 1.0 C A:PRO174 4.9 11.8 1.0 N A:ALA175 4.9 11.5 1.0 N A:PRO174 4.9 11.5 1.0 CA A:GLU172 4.9 8.5 1.0 O A:THR253 4.9 9.6 1.0

N.Strater, W.N.Lipscomb. Two-Metal Ion Mechanism of Bovine Lens Leucine Aminopeptidase: Active Site Solvent Structure and Binding Mode of L-Leucinal, A Gem-Diolate Transition State Analogue, By X-Ray Crystallography. Biochemistry V. 34 14792 1995.
ISSN: ISSN 0006-2960
PubMed: 7578088
DOI: 10.1021/BI00045A021