Magnesium in PDB 6wnq: E. Coli Atp Synthase State 2A

All present enzymatic activity of E. Coli Atp Synthase State 2A:
7.1.2.2;

The binding sites of Magnesium atom in the E. Coli Atp Synthase State 2A (pdb code 6wnq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the E. Coli Atp Synthase State 2A, PDB code: 6wnq:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the E. Coli Atp Synthase State 2A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Atp Synthase State 2A within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:56.1 occ:1.00 OG1 C:THR176 1.9 58.0 1.0 O2G C:ATP600 2.1 61.7 1.0 O2B C:ATP600 2.8 61.7 1.0 CB C:THR176 3.1 58.0 1.0 PG C:ATP600 3.5 61.7 1.0 CG2 C:THR176 3.6 58.0 1.0 PB C:ATP600 4.0 61.7 1.0 O1G C:ATP600 4.1 61.7 1.0 O3B C:ATP600 4.2 61.7 1.0 CA C:THR176 4.3 58.0 1.0 O2A C:ATP600 4.4 61.7 1.0 N C:THR176 4.5 58.0 1.0 OD1 C:ASP261 4.5 49.6 1.0 O3G C:ATP600 4.6 61.7 1.0 NE2 C:GLN200 4.7 54.0 1.0 OD2 C:ASP261 4.7 49.6 1.0 O1B C:ATP600 4.9 61.7 1.0 CD C:GLN200 5.0 54.0 1.0 CG C:ASP261 5.0 49.6 1.0

Magnesium binding site 2 out of 5 in the E. Coli Atp Synthase State 2A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli Atp Synthase State 2A within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:74.2 occ:1.00 O2B B:ATP600 1.8 74.8 1.0 O2G B:ATP600 1.8 74.8 1.0 O3B B:ATP600 1.8 74.8 1.0 PB B:ATP600 2.1 74.8 1.0 PG B:ATP600 2.1 74.8 1.0 O1A B:ATP600 2.4 74.8 1.0 O3A B:ATP600 2.9 74.8 1.0 PA B:ATP600 3.0 74.8 1.0 O1G B:ATP600 3.1 74.8 1.0 OG1 B:THR176 3.3 62.6 1.0 O3G B:ATP600 3.3 74.8 1.0 O1B B:ATP600 3.4 74.8 1.0 O2A B:ATP600 3.5 74.8 1.0 NH2 E:ARG342 3.6 73.7 1.0 CB B:THR176 4.0 62.6 1.0 O5' B:ATP600 4.4 74.8 1.0 N B:THR176 4.7 62.6 1.0 C5' B:ATP600 4.8 74.8 1.0 CZ E:ARG342 4.8 73.7 1.0 CA B:GLN172 4.9 73.1 1.0 CG2 B:THR176 5.0 62.6 1.0 CA B:THR176 5.0 62.6 1.0 N B:GLN172 5.0 73.1 1.0

Magnesium binding site 3 out of 5 in the E. Coli Atp Synthase State 2A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of E. Coli Atp Synthase State 2A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:82.0 occ:1.00 O2B A:ATP600 1.9 83.4 1.0 O2G A:ATP600 1.9 83.4 1.0 O1G A:ATP600 2.0 83.4 1.0 PG A:ATP600 2.3 83.4 1.0 OG1 A:THR176 2.5 73.2 1.0 PB A:ATP600 2.8 83.4 1.0 O3B A:ATP600 3.0 83.4 1.0 O1B A:ATP600 3.5 83.4 1.0 CB A:THR176 3.6 73.2 1.0 O3G A:ATP600 3.7 83.4 1.0 O2A A:ATP600 4.0 83.4 1.0 N A:THR176 4.2 73.2 1.0 O3A A:ATP600 4.2 83.4 1.0 NZ A:LYS175 4.4 73.9 1.0 CA A:THR176 4.5 73.2 1.0 PA A:ATP600 4.6 83.4 1.0 CG2 A:THR176 4.6 73.2 1.0 OD1 A:ASP261 4.7 61.5 1.0 CE A:LYS175 4.9 73.9 1.0 O1A A:ATP600 5.0 83.4 1.0

Magnesium binding site 4 out of 5 in the E. Coli Atp Synthase State 2A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of E. Coli Atp Synthase State 2A within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg501 b:58.0 occ:1.00 O3B F:ADP500 1.9 60.2 1.0 O2B F:ADP500 1.9 60.2 1.0 PB F:ADP500 2.2 60.2 1.0 O1B F:ADP500 3.1 60.2 1.0 OG1 F:THR156 3.5 54.6 1.0 NZ F:LYS155 3.5 50.5 1.0 O3A F:ADP500 3.6 60.2 1.0 NH1 F:ARG182 3.9 54.1 1.0 NH1 B:ARG376 4.2 59.7 1.0 CE F:LYS155 4.2 50.5 1.0 O2A F:ADP500 4.4 60.2 1.0 PA F:ADP500 4.6 60.2 1.0 NH2 F:ARG182 4.6 54.1 1.0 CB F:THR156 4.6 54.6 1.0 CG F:LYS155 4.7 50.5 1.0 OE2 F:GLU181 4.7 56.9 1.0 CZ F:ARG182 4.7 54.1 1.0 N F:GLY152 4.8 55.9 1.0 OE1 F:GLU181 4.8 56.9 1.0 CD F:GLU181 4.9 56.9 1.0

Magnesium binding site 5 out of 5 in the E. Coli Atp Synthase State 2A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of E. Coli Atp Synthase State 2A within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg502 b:89.9 occ:1.00 O4 D:PO4501 2.0 87.5 1.0 O3B D:ADP500 2.0 90.5 1.0 O1 D:PO4501 2.2 87.5 1.0 O1B D:ADP500 2.2 90.5 1.0 PB D:ADP500 2.3 90.5 1.0 P D:PO4501 2.5 87.5 1.0 O2B D:ADP500 2.9 90.5 1.0 O2 D:PO4501 3.4 87.5 1.0 NZ D:LYS155 3.6 87.5 1.0 CE D:LYS155 3.6 87.5 1.0 OG1 D:THR156 3.6 87.2 1.0 O3 D:PO4501 3.8 87.5 1.0 O3A D:ADP500 3.8 90.5 1.0 NE C:ARG376 3.9 74.9 1.0 O1A D:ADP500 4.4 90.5 1.0 CD C:ARG376 4.5 74.9 1.0 N D:GLY152 4.5 88.5 1.0 CZ C:ARG376 4.5 74.9 1.0 NH2 C:ARG376 4.6 74.9 1.0 NH1 D:ARG182 4.6 73.7 1.0 CB D:LYS155 4.6 87.5 1.0 PA D:ADP500 4.7 90.5 1.0 CD D:LYS155 4.7 87.5 1.0 N D:THR156 4.8 87.2 1.0 CB D:THR156 4.8 87.2 1.0 N D:LYS155 5.0 87.5 1.0

C.Robinson, A.G.Stewart, R.Ishmukhametov, R.Berry, M.Sobti, D.Wu, J.Walshe, Y.Zeng. Cryo-Em Structures Provide Insight Into How E. Coli F1FO Atp Synthase Accommodates Symmetry Mismatch Nat Commun 2020.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-020-16387-2