Magnesium in PDB 8f2k: Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A

All present enzymatic activity of Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A:
7.1.2.2;

The binding sites of Magnesium atom in the Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A (pdb code 8f2k). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A, PDB code: 8f2k:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:49.4 occ:1.00 OG1 A:THR178 2.1 65.1 1.0 O2B A:ATP600 2.1 80.5 1.0 O1G A:ATP600 2.1 85.6 1.0 CB A:THR178 3.1 61.6 1.0 PG A:ATP600 3.2 84.3 1.0 PB A:ATP600 3.2 63.4 1.0 O3B A:ATP600 3.2 72.9 1.0 O1A A:ATP600 3.9 76.9 1.0 CG2 A:THR178 4.0 64.5 1.0 OD2 A:ASP271 4.0 82.8 1.0 N A:THR178 4.2 55.8 1.0 CA A:THR178 4.2 53.6 1.0 O2G A:ATP600 4.2 76.4 1.0 O3A A:ATP600 4.2 65.0 1.0 O3G A:ATP600 4.2 69.6 1.0 O1B A:ATP600 4.2 69.2 1.0 NE2 A:GLN210 4.6 78.2 1.0 PA A:ATP600 4.7 74.5 1.0 CG A:ASP271 4.7 82.0 1.0 OD1 A:ASP271 4.8 83.7 1.0

Magnesium binding site 2 out of 5 in the Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:54.2 occ:1.00 OG1 B:THR178 2.1 71.5 1.0 O1B B:ATP600 2.1 76.7 1.0 O2G B:ATP600 2.2 80.2 1.0 CB B:THR178 3.1 64.0 1.0 PB B:ATP600 3.2 63.4 1.0 PG B:ATP600 3.4 78.3 1.0 O3B B:ATP600 3.4 70.8 1.0 OD2 B:ASP271 3.9 77.5 1.0 O3A B:ATP600 4.0 68.4 1.0 CG2 B:THR178 4.1 59.6 1.0 O1G B:ATP600 4.1 66.1 1.0 N B:THR178 4.1 48.9 1.0 CA B:THR178 4.2 51.8 1.0 O1A B:ATP600 4.2 70.8 1.0 O3G B:ATP600 4.5 76.5 1.0 O2B B:ATP600 4.5 72.9 1.0 OD1 B:ASP271 4.6 73.9 1.0 PA B:ATP600 4.6 68.2 1.0 CG B:ASP271 4.7 71.2 1.0 NE2 B:GLN210 4.7 70.2 1.0

Magnesium binding site 3 out of 5 in the Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:47.6 occ:1.00 O3G C:ATP600 2.0 84.0 1.0 OG1 C:THR178 2.0 65.8 1.0 O1B C:ATP600 2.0 80.6 1.0 OD2 C:ASP271 3.1 86.1 1.0 PB C:ATP600 3.1 74.7 1.0 CB C:THR178 3.2 69.1 1.0 PG C:ATP600 3.2 85.4 1.0 O3B C:ATP600 3.3 81.3 1.0 O3A C:ATP600 3.8 75.2 1.0 CG C:ASP271 4.0 82.4 1.0 O1G C:ATP600 4.0 77.5 1.0 N C:THR178 4.1 58.1 1.0 OD1 C:ASP271 4.1 84.8 1.0 CG2 C:THR178 4.1 68.1 1.0 CA C:THR178 4.2 60.4 1.0 O2G C:ATP600 4.3 67.1 1.0 O2B C:ATP600 4.5 73.0 1.0 NZ C:LYS177 4.9 77.9 1.0 PA C:ATP600 4.9 76.6 1.0 CE C:LYS177 5.0 68.7 1.0

Magnesium binding site 4 out of 5 in the Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg502 b:54.3 occ:1.00 O1G E:ATP501 2.0 78.3 1.0 OG1 E:THR164 2.0 58.3 1.0 O2B E:ATP501 2.1 71.4 1.0 PG E:ATP501 3.1 83.0 1.0 CB E:THR164 3.2 55.6 1.0 PB E:ATP501 3.3 72.8 1.0 O3B E:ATP501 3.3 61.7 1.0 OE2 E:GLU193 3.4 63.3 1.0 NH1 E:ARG190 3.9 48.8 1.0 OE1 E:GLU193 4.0 72.2 1.0 OE2 E:GLU189 4.0 67.8 1.0 O1A E:ATP501 4.0 71.2 1.0 CD E:GLU189 4.0 68.6 1.0 CG2 E:THR164 4.0 47.7 1.0 CD E:GLU193 4.1 69.0 1.0 OE1 E:GLU189 4.1 66.2 1.0 O3G E:ATP501 4.2 69.6 1.0 O2G E:ATP501 4.2 73.4 1.0 O3A E:ATP501 4.2 62.3 1.0 N E:THR164 4.3 41.2 1.0 CA E:THR164 4.3 42.0 1.0 O1B E:ATP501 4.3 72.2 1.0 OD1 E:ASP256 4.4 59.9 1.0 OD2 E:ASP256 4.6 69.7 1.0 CG E:GLU189 4.6 67.9 1.0 PA E:ATP501 4.7 58.0 1.0 NZ E:LYS163 4.7 56.3 1.0 NH2 B:ARG375 4.7 63.4 1.0 CG E:LYS163 4.8 50.8 1.0 CE E:LYS163 4.9 50.2 1.0 CG E:ASP256 5.0 68.0 1.0

Magnesium binding site 5 out of 5 in the Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure of Yeast F1-Atpase Determined with 100 Micromolar Cruentaren A within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg502 b:58.4 occ:1.00 O2B F:ATP501 2.0 68.4 1.0 O2G F:ATP501 2.0 67.7 1.0 OG1 F:THR164 2.1 67.5 1.0 CB F:THR164 3.2 64.0 1.0 PB F:ATP501 3.2 69.1 1.0 PG F:ATP501 3.3 76.8 1.0 OE2 F:GLU193 3.3 74.2 1.0 O3B F:ATP501 3.4 58.7 1.0 NH1 F:ARG190 3.9 62.3 1.0 N F:THR164 4.0 54.6 1.0 O1G F:ATP501 4.1 64.0 1.0 CD F:GLU193 4.2 76.9 1.0 CA F:THR164 4.2 50.5 1.0 CG2 F:THR164 4.2 57.2 1.0 O3A F:ATP501 4.2 60.2 1.0 OE1 F:GLU193 4.2 77.3 1.0 O1B F:ATP501 4.2 69.2 1.0 O1A F:ATP501 4.3 62.8 1.0 O3G F:ATP501 4.3 70.8 1.0 OD1 F:ASP256 4.5 80.0 1.0 OD2 F:ASP256 4.6 76.2 1.0 PA F:ATP501 4.6 55.9 1.0 O2A F:ATP501 4.8 71.0 1.0 NZ F:LYS163 4.9 66.0 1.0 NH1 C:ARG375 4.9 63.7 1.0 CE F:LYS163 4.9 55.7 1.0 CB F:LYS163 5.0 58.9 1.0 CG F:ASP256 5.0 81.5 1.0

X.Dou, H.Guo, T.Damico, L.Abdullah, C.Subramanian, B.A.Patel, M.Cohen, J.L.Rubinstein, B.S.J.Blagg. Late-Stage Diversification of Cruentaren A Based on Cryo-Em Structure with Atp Synthase To Be Published.