Magnesium in PDB 8eop: Cryo-Em Structure of Nanodisc Reconstituted Human ABCA7 Eq Mutant in Atp Bound Closed State

All present enzymatic activity of Cryo-Em Structure of Nanodisc Reconstituted Human ABCA7 Eq Mutant in Atp Bound Closed State:
7.6.2.1;

The binding sites of Magnesium atom in the Cryo-Em Structure of Nanodisc Reconstituted Human ABCA7 Eq Mutant in Atp Bound Closed State (pdb code 8eop). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryo-Em Structure of Nanodisc Reconstituted Human ABCA7 Eq Mutant in Atp Bound Closed State, PDB code: 8eop:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryo-Em Structure of Nanodisc Reconstituted Human ABCA7 Eq Mutant in Atp Bound Closed State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of Nanodisc Reconstituted Human ABCA7 Eq Mutant in Atp Bound Closed State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2208 b:56.3 occ:1.00 O1B A:ATP2210 2.0 66.8 1.0 O1G A:ATP2210 2.0 66.8 1.0 PB A:ATP2210 2.5 66.8 1.0 O3B A:ATP2210 2.5 66.8 1.0 PG A:ATP2210 2.5 66.8 1.0 CG2 A:THR848 2.7 62.6 1.0 O2B A:ATP2210 3.0 66.8 1.0 O2G A:ATP2210 3.0 66.8 1.0 OE1 A:GLN888 3.3 58.0 1.0 OG A:SER1927 3.4 55.1 1.0 OG1 A:THR848 3.6 62.6 1.0 CB A:THR848 3.8 62.6 1.0 O3A A:ATP2210 4.0 66.8 1.0 O3G A:ATP2210 4.0 66.8 1.0 CD A:GLN888 4.3 58.0 1.0 CG A:LYS847 4.3 67.1 1.0 N A:THR848 4.5 62.6 1.0 NE2 A:GLN888 4.7 58.0 1.0 CB A:SER1927 4.7 55.1 1.0 CA A:THR848 4.8 62.6 1.0 CD A:LYS847 4.8 67.1 1.0

Magnesium binding site 2 out of 2 in the Cryo-Em Structure of Nanodisc Reconstituted Human ABCA7 Eq Mutant in Atp Bound Closed State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of Nanodisc Reconstituted Human ABCA7 Eq Mutant in Atp Bound Closed State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2209 b:41.3 occ:1.00 OE1 A:GLN1874 2.1 42.8 1.0 OG1 A:THR1834 2.1 48.9 1.0 O2G A:ATP2207 2.2 61.0 1.0 O3B A:ATP2207 2.9 61.0 1.0 CD A:GLN1874 3.0 42.8 1.0 PG A:ATP2207 3.2 61.0 1.0 CB A:THR1834 3.4 48.9 1.0 NE2 A:GLN1874 3.4 42.8 1.0 NE2 A:GLN1951 3.5 43.5 1.0 CG2 A:THR1834 4.0 48.9 1.0 O3G A:ATP2207 4.1 61.0 1.0 PB A:ATP2207 4.1 61.0 1.0 O1B A:ATP2207 4.2 61.0 1.0 O1G A:ATP2207 4.3 61.0 1.0 CG A:GLN1874 4.3 42.8 1.0 CD A:GLN1951 4.4 43.5 1.0 CA A:THR1834 4.4 48.9 1.0 N A:THR1834 4.5 48.9 1.0 CB A:GLN1874 4.5 42.8 1.0 O3A A:ATP2207 4.6 61.0 1.0 OD2 A:ASP1950 4.9 43.1 1.0

L.T.M.Le, J.R.Thompson, S.Dehghani-Ghahnaviyeh, S.Pant, P.X.Dang, J.B.French, T.Kanikeyo, E.Tajkhorshid, A.Alam. Cryo-Em Structures of Human ABCA7 Provide Insights Into Its Phospholipid Translocation Mechanisms. Embo J. 11065 2022.
ISSN: ESSN 1460-2075
PubMed: 36484366
DOI: 10.15252/EMBJ.2022111065