Magnesium in PDB 1cow: Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B

All present enzymatic activity of Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B:
3.6.1.34;

The structure of Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B, PDB code: 1cow was solved by M.J.Van Raaij, J.P.Abrahams, A.G.W.Leslie, J.E.Walker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	283.400, 107.600, 140.200, 90.00, 90.00, 90.00
R / Rfree (%)	23.1 / n/a

The binding sites of Magnesium atom in the Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B (pdb code 1cow). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B, PDB code: 1cow:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:14.1 occ:1.00 O2G A:ANP600 1.9 24.9 1.0 O2B A:ANP600 2.1 17.3 1.0 O A:HOH669 2.4 65.5 1.0 OG1 A:THR176 2.4 25.2 1.0 PG A:ANP600 3.1 27.1 1.0 PB A:ANP600 3.1 21.4 1.0 N3B A:ANP600 3.2 25.6 1.0 CB A:THR176 3.4 23.2 1.0 O3G A:ANP600 3.8 29.7 1.0 O2A A:ANP600 3.9 27.4 1.0 O3A A:ANP600 4.2 23.6 1.0 N A:THR176 4.2 20.1 1.0 O1G A:ANP600 4.3 30.5 1.0 O1B A:ANP600 4.3 22.8 1.0 CG2 A:THR176 4.4 14.5 1.0 PA A:ANP600 4.4 24.5 1.0 CA A:THR176 4.4 23.1 1.0 O1A A:ANP600 4.5 24.0 1.0 OD2 A:ASP269 4.6 30.4 1.0 O A:HOH625 4.6 9.5 1.0 OD1 A:ASP269 4.8 30.6 1.0

Magnesium binding site 2 out of 5 in the Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:35.7 occ:1.00 OG1 B:THR176 1.9 32.4 1.0 O2G B:ANP600 2.2 35.0 1.0 O2B B:ANP600 2.3 18.6 1.0 CB B:THR176 3.1 22.0 1.0 O B:HOH632 3.4 40.3 1.0 OD1 B:ASP269 3.5 44.6 1.0 PB B:ANP600 3.6 21.2 1.0 PG B:ANP600 3.7 32.1 1.0 OD2 B:ASP269 3.7 33.0 1.0 N B:THR176 3.8 20.1 1.0 CA B:THR176 4.0 21.0 1.0 CG B:ASP269 4.0 34.2 1.0 N3B B:ANP600 4.1 24.2 1.0 CG2 B:THR176 4.2 12.6 1.0 O1G B:ANP600 4.2 37.1 1.0 O B:HOH636 4.4 51.1 1.0 O1B B:ANP600 4.5 24.5 1.0 OE1 B:GLN208 4.5 88.6 1.0 O3G B:ANP600 4.8 33.0 1.0 O3A B:ANP600 4.8 24.9 1.0 CB B:LYS175 4.8 26.4 1.0 NZ B:LYS175 4.9 24.7 1.0 O1A B:ANP600 4.9 30.9 1.0 O2A B:ANP600 4.9 26.5 1.0 C B:LYS175 4.9 22.0 1.0 NE2 B:GLN208 5.0 90.9 1.0

Magnesium binding site 3 out of 5 in the Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:19.3 occ:1.00 O2G C:ANP600 2.1 23.6 1.0 O2B C:ANP600 2.2 10.6 1.0 OG1 C:THR176 2.4 21.5 1.0 PG C:ANP600 3.4 20.5 1.0 CB C:THR176 3.5 10.7 1.0 PB C:ANP600 3.5 10.1 1.0 N3B C:ANP600 3.8 18.4 1.0 O2A C:ANP600 4.1 9.7 1.0 O3G C:ANP600 4.2 19.2 1.0 N C:THR176 4.2 8.9 1.0 O1B C:ANP600 4.2 7.2 1.0 OD2 C:ASP269 4.3 12.9 1.0 OD1 C:ASP269 4.3 27.5 1.0 CA C:THR176 4.4 8.4 1.0 O1G C:ANP600 4.5 19.5 1.0 CG2 C:THR176 4.5 15.7 1.0 CG C:ASP269 4.7 18.9 1.0 O3A C:ANP600 4.8 9.6 1.0 NZ C:LYS175 4.8 19.8 1.0 PA C:ANP600 4.9 11.7 1.0 O1A C:ANP600 4.9 16.7 1.0

Magnesium binding site 4 out of 5 in the Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg601 b:16.0 occ:1.00 O2B D:ADP600 2.3 30.8 1.0 OG1 D:THR163 2.3 37.0 1.0 CB D:THR163 3.4 24.0 1.0 NH1 D:ARG189 3.5 1.0 1.0 OE1 D:GLU188 3.6 25.4 1.0 PB D:ADP600 3.8 30.7 1.0 OE1 D:GLU192 3.8 53.2 1.0 OE2 D:GLU192 3.8 38.4 1.0 CD D:GLU192 4.2 41.0 1.0 O3B D:ADP600 4.2 32.9 1.0 CG2 D:THR163 4.3 27.1 1.0 O D:HOH656 4.3 17.1 1.0 OD1 D:ASP256 4.4 45.5 1.0 CD D:GLU188 4.4 26.2 1.0 N D:THR163 4.4 19.3 1.0 OD2 D:ASP256 4.4 54.4 1.0 CA D:THR163 4.5 21.2 1.0 O2A D:ADP600 4.5 16.7 1.0 O C:HOH658 4.6 19.0 1.0 O3A D:ADP600 4.6 27.8 1.0 O1A D:ADP600 4.7 21.7 1.0 NH1 C:ARG373 4.8 25.0 1.0 CZ D:ARG189 4.8 13.4 1.0 O1B D:ADP600 4.8 29.8 1.0 CG D:ASP256 4.9 42.9 1.0 PA D:ADP600 4.9 20.4 1.0 CG D:GLU188 5.0 27.4 1.0

Magnesium binding site 5 out of 5 in the Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Bovine Mitochondrial F1-Atpase Complexed with Aurovertin B within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg601 b:19.4 occ:1.00 O2G F:ANP600 1.9 28.6 1.0 O2B F:ANP600 2.3 23.8 1.0 OG1 F:THR163 2.4 8.5 1.0 PG F:ANP600 3.2 32.1 1.0 CB F:THR163 3.4 12.0 1.0 PB F:ANP600 3.4 25.7 1.0 OE1 F:GLU188 3.6 46.8 1.0 N3B F:ANP600 3.6 29.5 1.0 NH1 F:ARG189 3.8 30.6 1.0 OE2 F:GLU192 4.1 25.1 1.0 OD1 F:ASP256 4.1 26.8 1.0 O3G F:ANP600 4.1 34.5 1.0 O F:HOH627 4.1 41.7 1.0 N F:THR163 4.2 16.0 1.0 O1G F:ANP600 4.2 36.2 1.0 O1B F:ANP600 4.2 27.1 1.0 OD2 F:ASP256 4.3 29.6 1.0 O2A F:ANP600 4.4 25.4 1.0 CA F:THR163 4.4 12.8 1.0 CD F:GLU188 4.4 38.1 1.0 OE1 F:GLU192 4.4 34.0 1.0 CG2 F:THR163 4.6 5.3 1.0 CE F:LYS162 4.6 12.5 1.0 CG F:ASP256 4.7 18.5 1.0 CD F:GLU192 4.7 21.8 1.0 O3A F:ANP600 4.7 25.2 1.0 NH1 B:ARG373 4.8 12.9 1.0 O B:HOH620 5.0 21.4 1.0 PA F:ANP600 5.0 22.7 1.0

M.J.Van Raaij, J.P.Abrahams, A.G.Leslie, J.E.Walker. The Structure of Bovine F1-Atpase Complexed with the Antibiotic Inhibitor Aurovertin B. Proc.Natl.Acad.Sci.Usa V. 93 6913 1996.
ISSN: ISSN 0027-8424
PubMed: 8692918
DOI: 10.1073/PNAS.93.14.6913