Aluminium in PDB 1h8e: (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied)

All present enzymatic activity of (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied):
3.6.1.34;

The structure of (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied), PDB code: 1h8e was solved by R.I.Menz, J.E.Walker, A.G.W.Leslie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	13.5 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	267.700, 106.200, 138.300, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 26.4

The structure of (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied) also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Magnesium	(Mg)	6 atoms

The binding sites of Aluminium atom in the (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied) (pdb code 1h8e). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied), PDB code: 1h8e:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied)


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied) within 5.0Å range: probe atom residue distance (Å) B Occ D:Al620 b:37.9 occ:1.00 AL D:ALF620 0.0 37.9 1.0 F1 D:ALF620 1.8 40.4 1.0 F3 D:ALF620 1.8 39.2 1.0 F2 D:ALF620 1.8 37.9 1.0 F4 D:ALF620 1.8 41.3 1.0 O3B D:ADP600 2.1 29.6 1.0 O D:HOH2120 2.3 24.9 1.0 PB D:ADP600 3.3 27.4 1.0 O D:HOH2121 3.3 31.9 1.0 MG D:MG601 3.5 30.6 1.0 O2B D:ADP600 3.6 24.0 1.0 NZ D:LYS162 3.6 24.1 1.0 O D:HOH2155 3.7 31.3 1.0 OE1 D:GLU188 3.9 29.6 1.0 NH1 C:ARG373 4.0 23.9 1.0 O1B D:ADP600 4.0 27.1 1.0 N D:GLY159 4.0 25.2 1.0 CE D:LYS162 4.2 24.3 1.0 O C:SER344 4.4 23.7 1.0 CD1 D:TYR311 4.4 24.7 1.0 CB C:SER344 4.4 30.2 1.0 O3A D:ADP600 4.4 28.6 1.0 NH1 D:ARG189 4.5 27.7 1.0 CA C:SER344 4.5 24.5 1.0 NH2 D:ARG189 4.5 29.9 1.0 O D:HOH2122 4.5 28.1 1.0 CA D:ALA158 4.5 24.5 1.0 NH2 C:ARG373 4.6 23.1 1.0 CE1 D:TYR311 4.7 25.5 1.0 O D:HOH2125 4.7 25.9 1.0 CD D:GLU188 4.7 30.4 1.0 CZ C:ARG373 4.8 22.4 1.0 C D:ALA158 4.8 27.1 1.0 OE2 D:GLU188 4.8 35.9 1.0 CA D:GLY159 4.9 26.8 1.0 C C:SER344 4.9 23.5 1.0

Aluminium binding site 2 out of 2 in the (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied)


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of (Adp.ALF4)2(Adp.SO4) Bovine F1-Atpase (All Three Catalytic Sites Occupied) within 5.0Å range: probe atom residue distance (Å) B Occ F:Al620 b:33.9 occ:1.00 AL F:ALF620 0.0 33.9 1.0 F3 F:ALF620 1.8 34.5 1.0 F1 F:ALF620 1.8 33.2 1.0 F2 F:ALF620 1.8 35.7 1.0 F4 F:ALF620 1.8 34.0 1.0 O3B F:ADP600 2.0 25.3 1.0 O F:HOH2128 2.1 25.7 1.0 PB F:ADP600 3.3 25.1 1.0 MG F:MG601 3.5 28.5 1.0 O2B F:ADP600 3.7 26.9 1.0 O F:HOH2130 3.7 26.1 1.0 N F:GLY159 3.9 22.5 1.0 NZ F:LYS162 3.9 20.7 1.0 NH1 F:ARG189 3.9 21.8 1.0 O F:HOH2164 4.1 27.3 1.0 CB B:SER344 4.1 25.2 1.0 OE1 F:GLU188 4.1 25.3 1.0 CA B:SER344 4.1 25.0 1.0 O B:SER344 4.2 26.0 1.0 O1B F:ADP600 4.2 26.0 1.0 O F:HOH2134 4.2 25.6 1.0 O3A F:ADP600 4.2 25.9 1.0 NH2 F:ARG189 4.2 20.3 1.0 NH2 B:ARG373 4.3 25.5 1.0 O F:HOH2129 4.3 21.4 1.0 NH1 B:ARG373 4.4 29.3 1.0 CA F:ALA158 4.5 23.9 1.0 CE F:LYS162 4.6 19.5 1.0 C B:SER344 4.6 22.6 1.0 CZ F:ARG189 4.6 26.5 1.0 CA F:GLY159 4.6 22.6 1.0 C F:ALA158 4.7 23.0 1.0 CZ B:ARG373 4.8 31.1 1.0 CD1 F:TYR311 5.0 26.7 1.0 CD F:GLU188 5.0 31.8 1.0

R.I.Menz, J.E.Walker, A.G.W.Leslie. Structure of Bovine Mitochondrial F1-Atpase with Nucleotide Bound to All Three Catalytic Sites: Implications For the Mechanism of Rotary Catalysis Cell(Cambridge,Mass.) V. 106 331 2001.
ISSN: ISSN 0092-8674
PubMed: 11509182
DOI: 10.1016/S0092-8674(01)00452-4