Magnesium in PDB 7upt: Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation)

The binding sites of Magnesium atom in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation) (pdb code 7upt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation), PDB code: 7upt:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:134.2 occ:1.00 O3B B:ATP602 2.0 129.9 1.0 OG1 B:THR140 2.1 128.2 1.0 PG B:ATP602 2.4 129.9 1.0 O2G B:ATP602 2.4 129.9 1.0 O3G B:ATP602 2.5 129.9 1.0 O2B B:ATP602 2.8 129.9 1.0 CG2 B:THR140 2.9 128.2 1.0 PB B:ATP602 3.0 129.9 1.0 CB B:THR140 3.0 128.2 1.0 O3A B:ATP602 3.7 129.9 1.0 O1A B:ATP602 3.8 129.9 1.0 O1G B:ATP602 3.9 129.9 1.0 OD1 B:ASP192 3.9 134.1 1.0 CA B:THR140 4.1 128.2 1.0 N B:THR140 4.1 128.2 1.0 O D:ASP221 4.2 136.3 1.0 O1B B:ATP602 4.2 129.9 1.0 OD2 B:ASP192 4.3 134.1 1.0 PA B:ATP602 4.4 129.9 1.0 OE1 B:GLN193 4.5 131.4 1.0 CG B:ASP192 4.5 134.1 1.0 CA D:GLY222 4.9 140.6 1.0 OD1 D:ASP221 4.9 136.3 1.0

Magnesium binding site 2 out of 5 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:118.3 occ:1.00 O3B C:ATP602 2.0 129.9 1.0 OG1 C:THR140 2.0 130.5 1.0 O2G C:ATP602 2.3 129.9 1.0 PG C:ATP602 2.6 129.9 1.0 CB C:THR140 2.7 130.5 1.0 PB C:ATP602 3.0 129.9 1.0 O3G C:ATP602 3.1 129.9 1.0 O2B C:ATP602 3.2 129.9 1.0 NH2 B:ARG250 3.2 126.4 1.0 CG2 C:THR140 3.3 130.5 1.0 O3A C:ATP602 3.5 129.9 1.0 OD2 C:ASP192 3.8 128.6 1.0 O1G C:ATP602 3.9 129.9 1.0 O1A C:ATP602 3.9 129.9 1.0 CA C:THR140 4.1 130.5 1.0 CZ B:ARG250 4.2 126.4 1.0 O B:ASP221 4.3 133.1 1.0 O1B C:ATP602 4.3 129.9 1.0 N C:THR140 4.4 130.5 1.0 PA C:ATP602 4.4 129.9 1.0 OD1 C:ASP192 4.5 128.6 1.0 OD1 B:ASP221 4.6 133.1 1.0 CG C:ASP192 4.6 128.6 1.0 CA B:GLY222 4.6 136.3 1.0 NH1 B:ARG250 4.6 126.4 1.0 OE1 C:GLN193 4.9 123.2 1.0 C B:ASP221 4.9 133.1 1.0

Magnesium binding site 3 out of 5 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg502 b:160.3 occ:1.00 O1A D:ATP501 2.0 152.0 1.0 O3A D:ATP501 2.1 152.0 1.0 OG1 D:THR140 2.2 141.6 1.0 O3B D:ATP501 2.3 152.0 1.0 PB D:ATP501 2.4 152.0 1.0 O2B D:ATP501 2.5 152.0 1.0 PA D:ATP501 2.5 152.0 1.0 CB D:THR140 2.6 141.6 1.0 N D:THR140 3.4 141.6 1.0 O2A D:ATP501 3.6 152.0 1.0 CA D:THR140 3.6 141.6 1.0 OD1 A:ASP221 3.6 174.2 1.0 O5' D:ATP501 3.6 152.0 1.0 PG D:ATP501 3.7 152.0 1.0 CG2 D:THR140 3.8 141.6 1.0 O1B D:ATP501 3.8 152.0 1.0 OD2 A:ASP221 3.9 174.2 1.0 CG A:ASP221 4.0 174.2 1.0 O3G D:ATP501 4.0 152.0 1.0 O2G D:ATP501 4.2 152.0 1.0 NH1 A:ARG249 4.2 163.1 1.0 C5' D:ATP501 4.4 152.0 1.0 C D:THR140 4.6 141.6 1.0 N D:LEU141 4.7 144.9 1.0 C D:LYS139 4.7 137.8 1.0 O1G D:ATP501 4.8 152.0 1.0 NH1 A:ARG250 4.9 169.5 1.0 CB D:LYS139 4.9 137.8 1.0

Magnesium binding site 4 out of 5 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg502 b:152.9 occ:1.00 OG1 E:THR140 2.0 140.9 1.0 O3G E:ATP501 2.1 141.5 1.0 O2G E:ATP501 2.3 141.5 1.0 PG E:ATP501 2.3 141.5 1.0 O3B E:ATP501 2.4 141.5 1.0 OD1 E:ASP192 2.7 141.8 1.0 O2B E:ATP501 3.1 141.5 1.0 OD2 E:ASP192 3.2 141.8 1.0 CG E:ASP192 3.3 141.8 1.0 CB E:THR140 3.3 140.9 1.0 PB E:ATP501 3.4 141.5 1.0 OE1 E:GLN193 3.8 142.1 1.0 O1G E:ATP501 3.9 141.5 1.0 CG2 E:THR140 4.1 140.9 1.0 CA E:THR140 4.3 140.9 1.0 O1B E:ATP501 4.4 141.5 1.0 N E:THR140 4.4 140.9 1.0 O3A E:ATP501 4.4 141.5 1.0 NE2 E:GLN193 4.5 142.1 1.0 CD E:GLN193 4.6 142.1 1.0 CB E:ASP192 4.7 141.8 1.0 CA C:GLY222 4.8 143.7 1.0 NH2 C:ARG250 4.9 130.7 1.0

Magnesium binding site 5 out of 5 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg601 b:194.9 occ:1.00 OG1 F:THR140 2.0 196.8 1.0 O3B F:ATP602 2.1 195.7 1.0 O3G F:ATP602 2.3 195.7 1.0 PG F:ATP602 2.4 195.7 1.0 O2G F:ATP602 2.5 195.7 1.0 O2B F:ATP602 2.7 195.7 1.0 PB F:ATP602 2.9 195.7 1.0 CB F:THR140 3.1 196.8 1.0 OD2 F:ASP192 3.3 189.7 1.0 O1G F:ATP602 3.8 195.7 1.0 O3A F:ATP602 3.9 195.7 1.0 CG2 F:THR140 3.9 196.8 1.0 OD1 F:ASP192 4.0 189.7 1.0 CG F:ASP192 4.1 189.7 1.0 O1B F:ATP602 4.1 195.7 1.0 CA F:THR140 4.3 196.8 1.0 N F:THR140 4.4 196.8 1.0 OE1 F:GLN193 4.5 187.6 1.0 NH2 E:ARG250 4.6 168.2 1.0 O1A F:ATP602 4.7 195.7 1.0 PA F:ATP602 4.9 195.7 1.0

L.Wang, H.Toutkoushian, V.Belyy, C.Y.Kokontis, P.Walter. Conserved Structural Elements Specialize ATAD1 As A Membrane Protein Extraction Machine. Elife V. 11 2022.
ISSN: ESSN 2050-084X
PubMed: 35550246
DOI: 10.7554/ELIFE.73941