Aluminium in PDB 2hf7: Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex)

All present enzymatic activity of Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex):
3.1.3.2;

The structure of Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex), PDB code: 2hf7 was solved by R.Leone, V.Calderone, E.Cappelletti, M.Benvenuti, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.16 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.430, 66.484, 91.624, 90.00, 121.12, 90.00
R / Rfree (%)	17.1 / 19.6

The structure of Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex) also contains other interesting chemical elements:

Fluorine	(F)	6 atoms
Magnesium	(Mg)	2 atoms

The binding sites of Aluminium atom in the Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex) (pdb code 2hf7). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex), PDB code: 2hf7:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex)


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Al800 b:10.5 occ:1.00 AL A:AF3800 0.0 10.5 1.0 F3 A:AF3800 1.8 7.5 1.0 F1 A:AF3800 1.8 6.2 1.0 F2 A:AF3800 1.8 8.9 1.0 O A:HOH1101 2.1 8.8 1.0 OD1 A:ASP44 2.1 5.7 1.0 CG A:ASP44 3.1 5.6 1.0 MG A:MG700 3.4 6.1 1.0 OD2 A:ASP44 3.4 5.2 1.0 OG1 A:THR112 3.6 6.4 1.0 N A:ASP46 3.7 4.9 1.0 O A:HOH810 3.7 4.0 1.0 NZ A:LYS152 3.8 6.8 1.0 O A:HOH858 3.9 16.5 1.0 OD2 A:ASP46 3.9 6.7 1.0 O A:HOH1070 3.9 23.3 1.0 N A:GLY113 3.9 5.8 1.0 CB A:ASP46 4.0 5.3 1.0 N A:ILE45 4.1 5.1 1.0 CA A:THR112 4.2 5.8 1.0 CG A:ASP46 4.3 5.8 1.0 CB A:THR112 4.4 5.5 1.0 CA A:ASP46 4.4 4.5 1.0 O A:ASP46 4.4 4.4 1.0 CB A:ASP44 4.5 4.6 1.0 O A:HOH1017 4.5 24.5 1.0 C A:THR112 4.6 5.8 1.0 O A:HOH806 4.7 4.1 1.0 C A:ILE45 4.7 5.5 1.0 CA A:ILE45 4.8 5.0 1.0 O A:HOH1038 4.8 29.0 1.0 CE A:LYS152 4.8 6.8 1.0 CA A:ASP44 4.9 4.7 1.0 C A:ASP46 4.9 4.2 1.0 CA A:GLY113 4.9 6.5 1.0 C A:ASP44 4.9 5.3 1.0

Aluminium binding site 2 out of 2 in the Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex)


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Transition State Analogue of Apha Class B Acid Phosphatase/Phosphotransferase (Aluminium Fluoride Complex) within 5.0Å range: probe atom residue distance (Å) B Occ B:Al801 b:19.1 occ:1.00 AL B:AF3801 0.0 19.1 1.0 F3 B:AF3801 1.8 12.1 1.0 F1 B:AF3801 1.8 16.6 1.0 F2 B:AF3801 1.8 10.4 1.0 OD1 B:ASP44 2.0 5.0 1.0 O B:HOH1112 2.3 27.2 1.0 CG B:ASP44 3.1 5.8 1.0 OD2 B:ASP44 3.5 4.2 1.0 O B:HOH933 3.5 19.6 1.0 MG B:MG701 3.6 7.0 1.0 O B:HOH916 3.7 18.1 1.0 N B:ASP46 3.7 5.2 1.0 NZ B:LYS152 3.8 12.4 1.0 OG1 B:THR112 3.8 9.1 1.0 O B:HOH816 3.8 5.7 1.0 OD2 B:ASP46 3.9 8.3 1.0 N B:ILE45 4.0 5.1 1.0 O B:HOH967 4.1 22.9 1.0 CB B:ASP46 4.1 5.2 1.0 N B:GLY113 4.1 7.7 1.0 CB B:ASP44 4.4 5.3 1.0 CG B:ASP46 4.4 6.6 1.0 CA B:ASP46 4.4 5.2 1.0 CA B:THR112 4.4 7.6 1.0 O B:ASP46 4.5 5.0 1.0 CB B:THR112 4.6 7.8 1.0 C B:ILE45 4.7 5.2 1.0 CA B:ILE45 4.7 5.3 1.0 O B:HOH813 4.7 5.8 1.0 CA B:ASP44 4.8 5.5 1.0 C B:ASP44 4.8 5.8 1.0 C B:THR112 4.8 7.9 1.0 CE B:LYS152 4.9 16.0 1.0 CB B:ILE45 4.9 5.1 1.0 C B:ASP46 5.0 4.8 1.0 O B:HOH1019 5.0 33.5 1.0

R.Leone, V.Calderone, E.Cappelletti, M.Benvenuti, S.Mangani. N/A N/A.