Magnesium in PDB 5uie: VPS4-VTA1 Complex

The structure of VPS4-VTA1 Complex also contains other interesting chemical elements:

Fluorine

(F)

9 atoms

The binding sites of Magnesium atom in the VPS4-VTA1 Complex (pdb code 5uie). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the VPS4-VTA1 Complex, PDB code: 5uie:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the VPS4-VTA1 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of VPS4-VTA1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:0.1 occ:1.00 F1 A:BEF502 2.0 0.1 1.0 O3B A:ADP501 3.1 0.1 1.0 OD2 A:ASP232 3.2 0.8 1.0 BE A:BEF502 3.2 0.1 1.0 F3 A:BEF502 3.2 0.1 1.0 OD1 A:ASP232 3.3 0.8 1.0 CB A:SER180 3.6 98.6 1.0 CG A:ASP232 3.6 0.8 1.0 F2 A:BEF502 4.3 0.1 1.0 O1B A:ADP501 4.3 0.1 1.0 OG A:SER180 4.4 98.6 1.0 PB A:ADP501 4.4 0.1 1.0 N A:SER180 4.4 98.6 1.0 OE2 A:GLU233 4.5 0.0 1.0 CA A:SER180 4.5 98.6 1.0 NH2 B:ARG289 4.8 95.4 1.0

Magnesium binding site 2 out of 3 in the VPS4-VTA1 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of VPS4-VTA1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:0.6 occ:1.00 F1 C:BEF501 2.0 0.6 1.0 O2B B:ADP501 3.1 0.6 1.0 OD2 B:ASP232 3.1 97.4 1.0 BE C:BEF501 3.2 0.6 1.0 OD1 B:ASP232 3.2 97.4 1.0 F3 C:BEF501 3.3 0.6 1.0 O3B B:ADP501 3.5 0.6 1.0 CG B:ASP232 3.5 97.4 1.0 CB B:SER180 3.6 88.7 1.0 PB B:ADP501 3.6 0.6 1.0 O1B B:ADP501 3.9 0.6 1.0 OG B:SER180 4.2 88.7 1.0 F2 C:BEF501 4.5 0.6 1.0 NH2 C:ARG289 4.5 80.3 1.0 CA B:SER180 4.6 88.7 1.0 N B:SER180 4.6 88.7 1.0 OE2 B:GLU233 4.8 0.4 1.0

Magnesium binding site 3 out of 3 in the VPS4-VTA1 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of VPS4-VTA1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg504 b:0.6 occ:1.00 F1 C:BEF503 2.0 0.6 1.0 O2B C:ADP502 3.1 0.6 1.0 OD1 C:ASP232 3.1 81.1 1.0 BE C:BEF503 3.2 0.6 1.0 OD2 C:ASP232 3.2 81.1 1.0 F3 C:BEF503 3.3 0.6 1.0 CG C:ASP232 3.6 81.1 1.0 NH2 D:ARG289 4.0 82.4 1.0 OE2 C:GLU233 4.1 90.2 1.0 O3B C:ADP502 4.3 0.6 1.0 CB C:SER180 4.3 83.4 1.0 F2 C:BEF503 4.3 0.6 1.0 PB C:ADP502 4.3 0.6 1.0 CG C:GLU233 4.5 90.2 1.0 CD C:GLU233 4.7 90.2 1.0 OG C:SER180 4.9 83.4 1.0

N.Monroe, H.Han, P.S.Shen, W.I.Sundquist, C.P.Hill. Structural Basis of Protein Translocation By the VPS4-VTA1 Aaa Atpase. Elife V. 6 2017.
ISSN: ESSN 2050-084X
PubMed: 28379137
DOI: 10.7554/ELIFE.24487