Magnesium in PDB 6fkh: Chloroplast F1FO Conformation 2

All present enzymatic activity of Chloroplast F1FO Conformation 2:
3.6.3.14;

The binding sites of Magnesium atom in the Chloroplast F1FO Conformation 2 (pdb code 6fkh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Chloroplast F1FO Conformation 2, PDB code: 6fkh:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Chloroplast F1FO Conformation 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Chloroplast F1FO Conformation 2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:72.9 occ:1.00 O3G C:ATP602 2.1 78.9 1.0 O2B C:ATP602 2.1 78.9 1.0 OG1 C:THR177 2.1 69.4 1.0 PG C:ATP602 3.2 78.9 1.0 CB C:THR177 3.4 69.4 1.0 O1G C:ATP602 3.4 78.9 1.0 PB C:ATP602 3.4 78.9 1.0 O3B C:ATP602 3.7 78.9 1.0 OD1 C:ASP262 4.1 64.8 1.0 N C:THR177 4.2 69.4 1.0 CG2 C:THR177 4.2 69.4 1.0 O1B C:ATP602 4.3 78.9 1.0 CA C:THR177 4.3 69.4 1.0 NE2 C:GLN201 4.4 71.2 1.0 O2G C:ATP602 4.4 78.9 1.0 O3A C:ATP602 4.6 78.9 1.0 O2A C:ATP602 4.6 78.9 1.0 OD2 C:ASP262 4.7 64.8 1.0 NZ C:LYS176 4.7 68.4 1.0 CG C:ASP262 4.8 64.8 1.0 PA C:ATP602 4.9 78.9 1.0

Magnesium binding site 2 out of 5 in the Chloroplast F1FO Conformation 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Chloroplast F1FO Conformation 2 within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg601 b:79.8 occ:1.00 OG1 E:THR177 1.8 77.1 1.0 O2G E:ATP600 2.0 87.6 1.0 O2B E:ATP600 2.7 87.6 1.0 CB E:THR177 3.1 77.1 1.0 PG E:ATP600 3.5 87.6 1.0 NE2 E:GLN201 3.6 74.3 1.0 CG2 E:THR177 3.6 77.1 1.0 PB E:ATP600 4.0 87.6 1.0 O3B E:ATP600 4.1 87.6 1.0 CA E:THR177 4.2 77.1 1.0 O3G E:ATP600 4.3 87.6 1.0 O2A E:ATP600 4.3 87.6 1.0 OD1 E:ASP262 4.4 67.0 1.0 O1G E:ATP600 4.4 87.6 1.0 CD E:GLN201 4.4 74.3 1.0 N E:THR177 4.4 77.1 1.0 OD2 E:ASP262 4.7 67.0 1.0 OG E:SER205 4.7 76.7 1.0 OE1 E:GLN201 4.8 74.3 1.0 O3A E:ATP600 4.9 87.6 1.0 CG E:ASP262 4.9 67.0 1.0 PA E:ATP600 5.0 87.6 1.0

Magnesium binding site 3 out of 5 in the Chloroplast F1FO Conformation 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Chloroplast F1FO Conformation 2 within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg601 b:74.1 occ:1.00 OG1 F:THR179 2.0 74.3 1.0 O2B F:ADP600 2.1 79.4 1.0 O3B F:ADP600 2.4 79.4 1.0 PB F:ADP600 2.6 79.4 1.0 CB F:THR179 3.3 74.3 1.0 O1B F:ADP600 3.5 79.4 1.0 NH1 F:ARG205 3.5 71.9 1.0 OE2 F:GLU208 3.8 77.8 1.0 O3A F:ADP600 4.0 79.4 1.0 N F:THR179 4.0 74.3 1.0 OE1 F:GLU204 4.1 75.2 1.0 CA F:THR179 4.2 74.3 1.0 CG2 F:THR179 4.3 74.3 1.0 O2A F:ADP600 4.3 79.4 1.0 PA F:ADP600 4.4 79.4 1.0 OD1 F:ASP273 4.5 25.7 1.0 O1A F:ADP600 4.5 79.4 1.0 OE1 F:GLU208 4.6 77.8 1.0 CD F:GLU208 4.6 77.8 1.0 CZ F:ARG205 4.7 71.9 1.0 CE F:LYS178 4.8 70.5 1.0 OD2 F:ASP273 4.8 24.8 1.0 CB F:LYS178 4.9 70.5 1.0

Magnesium binding site 4 out of 5 in the Chloroplast F1FO Conformation 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Chloroplast F1FO Conformation 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:87.6 occ:1.00 OG1 A:THR177 1.9 75.4 1.0 O3G A:ATP600 1.9 90.4 1.0 O2B A:ATP600 2.2 90.4 1.0 CB A:THR177 3.2 75.4 1.0 PG A:ATP600 3.3 90.4 1.0 PB A:ATP600 3.5 90.4 1.0 O3B A:ATP600 3.7 90.4 1.0 CG2 A:THR177 4.0 75.4 1.0 NE2 A:GLN201 4.0 74.5 1.0 O2A A:ATP600 4.1 90.4 1.0 OD1 A:ASP262 4.2 67.7 1.0 O1G A:ATP600 4.2 90.4 1.0 CA A:THR177 4.2 75.4 1.0 N A:THR177 4.3 75.4 1.0 O2G A:ATP600 4.4 90.4 1.0 O3A A:ATP600 4.5 90.4 1.0 O1B A:ATP600 4.5 90.4 1.0 PA A:ATP600 4.7 90.4 1.0 OD2 A:ASP262 4.8 67.7 1.0 CG A:ASP262 4.9 67.7 1.0

Magnesium binding site 5 out of 5 in the Chloroplast F1FO Conformation 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Chloroplast F1FO Conformation 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:64.1 occ:1.00 OG1 B:THR179 1.9 68.3 1.0 O2B B:ADP501 2.3 70.5 1.0 CB B:THR179 3.4 68.3 1.0 OE1 B:GLU204 3.4 74.4 1.0 NH1 B:ARG205 3.7 69.6 1.0 PB B:ADP501 3.8 70.5 1.0 OD1 B:ASP273 3.8 25.4 1.0 OE1 B:GLU208 3.8 75.1 1.0 CD B:GLU204 3.8 74.4 1.0 OE2 B:GLU204 4.1 74.4 1.0 CG2 B:THR179 4.1 68.3 1.0 OD2 B:ASP273 4.2 26.4 1.0 CA B:THR179 4.2 68.3 1.0 N B:THR179 4.2 68.3 1.0 OE2 B:GLU208 4.3 75.1 1.0 CG B:ASP273 4.4 24.4 1.0 CD B:GLU208 4.5 75.1 1.0 O3B B:ADP501 4.5 70.5 1.0 O1B B:ADP501 4.6 70.5 1.0 CG B:GLU204 4.7 74.4 1.0 O3A B:ADP501 4.7 70.5 1.0 CE B:LYS178 4.7 67.1 1.0 CZ B:ARG205 4.9 69.6 1.0 O2A B:ADP501 5.0 70.5 1.0 CB B:LYS178 5.0 67.1 1.0

A.Hahn, J.Vonck, D.J.Mills, T.Meier, W.Kuhlbrandt. Structure, Mechanism, and Regulation of the Chloroplast Atp Synthase. Science V. 360 2018.
ISSN: ESSN 1095-9203
PubMed: 29748256
DOI: 10.1126/SCIENCE.AAT4318