Zinc in PDB 1ft7: Aap Complexed with L-Leucinephosphonic Acid

All present enzymatic activity of Aap Complexed with L-Leucinephosphonic Acid:
3.4.11.10;

The structure of Aap Complexed with L-Leucinephosphonic Acid, PDB code: 1ft7 was solved by C.Stamper, B.Bennett, R.Holz, G.Petsko, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	107.000, 107.000, 102.000, 90.00, 90.00, 120.00
R / Rfree (%)	19.8 / 23.2

The structure of Aap Complexed with L-Leucinephosphonic Acid also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Zinc atom in the Aap Complexed with L-Leucinephosphonic Acid (pdb code 1ft7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Aap Complexed with L-Leucinephosphonic Acid, PDB code: 1ft7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Aap Complexed with L-Leucinephosphonic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aap Complexed with L-Leucinephosphonic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:10.8 occ:1.00 O1 A:PLU500 1.9 13.0 1.0 OD2 A:ASP117 1.9 5.9 1.0 OE2 A:GLU152 2.0 6.9 1.0 NE2 A:HIS256 2.1 10.9 1.0 OE1 A:GLU152 2.4 6.5 1.0 CD A:GLU152 2.5 8.3 1.0 CD2 A:HIS256 2.9 6.7 1.0 CG A:ASP117 3.0 8.0 1.0 P A:PLU500 3.1 13.5 1.0 CE1 A:HIS256 3.2 14.9 1.0 O3 A:PLU500 3.4 11.9 1.0 OD1 A:ASP117 3.5 11.7 1.0 ZN A:ZN502 3.9 12.7 1.0 O A:HOH644 3.9 11.7 1.0 CG A:GLU152 4.0 5.4 1.0 O A:HOH652 4.0 20.6 1.0 N A:PLU500 4.1 10.5 1.0 O2 A:PLU500 4.1 7.4 1.0 O A:HOH627 4.1 13.2 1.0 CG A:HIS256 4.1 11.7 1.0 ND1 A:HIS256 4.2 14.2 1.0 CB A:ASP117 4.3 3.4 1.0 CA A:PLU500 4.3 11.1 1.0 CD1 A:ILE255 4.5 10.1 1.0 CG2 A:THR101 4.6 6.2 1.0 CE1 A:HIS97 4.8 9.3 1.0 CB A:GLU152 4.9 10.3 1.0 NE2 A:HIS97 4.9 7.0 1.0 OE1 A:GLU151 4.9 8.8 1.0

Zinc binding site 2 out of 2 in the Aap Complexed with L-Leucinephosphonic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aap Complexed with L-Leucinephosphonic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:12.7 occ:1.00 OD1 A:ASP117 2.0 11.7 1.0 N A:PLU500 2.1 10.5 1.0 OD1 A:ASP179 2.2 8.5 1.0 NE2 A:HIS97 2.2 7.0 1.0 O3 A:PLU500 2.2 11.9 1.0 OD2 A:ASP179 2.4 3.8 1.0 CG A:ASP179 2.6 7.8 1.0 CA A:PLU500 3.0 11.1 1.0 P A:PLU500 3.0 13.5 1.0 CG A:ASP117 3.0 8.0 1.0 CE1 A:HIS97 3.2 9.3 1.0 CD2 A:HIS97 3.2 5.1 1.0 OD2 A:ASP117 3.4 5.9 1.0 O1 A:PLU500 3.5 13.0 1.0 OE2 A:GLU152 3.8 6.9 1.0 ZN A:ZN501 3.9 10.8 1.0 OE1 A:GLU151 4.0 8.8 1.0 CB A:ASP179 4.1 7.6 1.0 ND1 A:HIS97 4.3 6.6 1.0 CB A:ASP118 4.3 6.5 1.0 CB A:ASP117 4.3 3.4 1.0 OE2 A:GLU151 4.3 9.5 1.0 CG A:HIS97 4.3 6.9 1.0 CD A:GLU151 4.4 10.7 1.0 CB A:PLU500 4.4 12.1 1.0 O2 A:PLU500 4.4 7.4 1.0 CD A:GLU152 4.5 8.3 1.0 CA A:ASP117 4.7 6.3 1.0 OG A:SER228 4.7 7.0 1.0 CG A:MET180 4.8 4.0 1.0 SD A:MET180 4.8 12.6 1.0 CG A:ASP118 4.8 8.3 1.0 CA A:ASP179 4.8 7.5 1.0 OE1 A:GLU152 4.9 6.5 1.0 C A:ASP117 4.9 6.3 1.0

C.Stamper, B.Bennett, T.Edwards, R.C.Holz, D.Ringe, G.Petsko. Inhibition of the Aminopeptidase From Aeromonas Proteolytica By L-Leucinephosphonic Acid. Spectroscopic and Crystallographic Characterization of the Transition State of Peptide Hydrolysis. Biochemistry V. 40 7035 2001.
ISSN: ISSN 0006-2960
PubMed: 11401547
DOI: 10.1021/BI0100891