Potassium 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:

Zinc

(Zn)

2 atoms

The binding sites of Potassium atom in the Aap Complexed with L-Leucinephosphonic Acid (pdb code 1ft7). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Aap Complexed with L-Leucinephosphonic Acid, PDB code: 1ft7:

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Aap Complexed with L-Leucinephosphonic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:K600 b:30.2 occ:1.00 O2 A:PLU500 2.6 7.4 1.0 OE2 A:GLU151 2.6 9.5 1.0 O A:HOH700 2.7 19.8 1.0 O A:CYS227 2.8 9.7 1.0 O A:HOH699 2.8 19.6 1.0 C A:CYS227 3.3 6.8 1.0 CD2 A:LEU155 3.4 14.3 1.0 CD A:GLU151 3.5 10.7 1.0 P A:PLU500 3.7 13.5 1.0 O3 A:PLU500 3.8 11.9 1.0 N A:SER228 3.9 7.9 1.0 O A:HOH615 3.9 14.5 1.0 OE1 A:GLU151 3.9 8.8 1.0 CA A:SER228 3.9 6.3 1.0 O A:HOH627 4.1 13.2 1.0 CA A:CYS227 4.1 8.4 1.0 O A:GLU151 4.2 5.5 1.0 CA A:PLU500 4.4 11.1 1.0 O A:ALA226 4.4 11.7 1.0 CG A:LEU155 4.5 14.1 1.0 CG A:GLU151 4.5 6.4 1.0 O A:HOH701 4.9 41.5 1.0 CB A:SER228 4.9 7.0 1.0 C A:SER228 4.9 4.0 1.0 O1 A:PLU500 4.9 13.0 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