Magnesium in PDB 5nug: Motor Domains From Human Cytoplasmic Dynein-1 in the Phi-Particle Conformation

The binding sites of Magnesium atom in the Motor Domains From Human Cytoplasmic Dynein-1 in the Phi-Particle Conformation (pdb code 5nug). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Motor Domains From Human Cytoplasmic Dynein-1 in the Phi-Particle Conformation, PDB code: 5nug:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Motor Domains From Human Cytoplasmic Dynein-1 in the Phi-Particle Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Motor Domains From Human Cytoplasmic Dynein-1 in the Phi-Particle Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg4803 b:34.0 occ:1.00 O2B A:ATP4802 1.7 50.1 1.0 O3G A:ATP4802 1.8 54.1 1.0 OG A:SER2231 1.9 68.9 1.0 OE2 A:GLU2344 2.3 64.8 1.0 PG A:ATP4802 2.4 54.5 1.0 PB A:ATP4802 2.5 49.0 1.0 O1G A:ATP4802 2.6 53.7 1.0 O3B A:ATP4802 2.7 51.8 1.0 O1B A:ATP4802 3.1 48.3 1.0 CB A:SER2231 3.2 69.9 1.0 NZ A:LYS2230 3.3 68.2 1.0 CD A:GLU2344 3.4 64.4 1.0 OE2 A:GLU2688 3.6 95.3 1.0 N A:SER2231 3.8 61.4 1.0 O2G A:ATP4802 3.8 53.5 1.0 O3A A:ATP4802 3.9 50.8 1.0 NH1 A:ARG2729 4.0 91.5 1.0 CA A:SER2231 4.0 66.9 1.0 OE1 A:GLU2344 4.2 65.7 1.0 NH2 A:ARG2684 4.2 58.0 1.0 CG A:GLU2344 4.3 60.0 1.0 OD2 A:ASP2304 4.3 77.8 1.0 OE1 A:GLU2688 4.4 0.4 1.0 CD A:GLU2688 4.4 99.0 1.0 O1A A:ATP4802 4.5 54.4 1.0 PA A:ATP4802 4.5 54.1 1.0 OD1 A:ASP2304 4.5 77.1 1.0 O2A A:ATP4802 4.6 53.7 1.0 NH2 A:ARG2726 4.6 64.8 1.0 CB A:LYS2230 4.6 66.7 1.0 CE A:LYS2230 4.7 68.8 1.0 CG A:ASP2304 4.9 76.6 1.0 C A:LYS2230 4.9 61.6 1.0

Magnesium binding site 2 out of 2 in the Motor Domains From Human Cytoplasmic Dynein-1 in the Phi-Particle Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Motor Domains From Human Cytoplasmic Dynein-1 in the Phi-Particle Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg4803 b:34.0 occ:1.00 O2B B:ATP4802 1.7 50.1 1.0 O3G B:ATP4802 1.8 54.1 1.0 OG B:SER2231 1.9 68.9 1.0 OE2 B:GLU2344 2.3 64.8 1.0 PG B:ATP4802 2.4 54.5 1.0 PB B:ATP4802 2.5 49.0 1.0 O1G B:ATP4802 2.6 53.7 1.0 O3B B:ATP4802 2.7 51.8 1.0 O1B B:ATP4802 3.1 48.3 1.0 CB B:SER2231 3.2 69.9 1.0 NZ B:LYS2230 3.3 68.2 1.0 CD B:GLU2344 3.4 64.4 1.0 OE2 B:GLU2688 3.6 95.3 1.0 N B:SER2231 3.8 61.4 1.0 O2G B:ATP4802 3.8 53.5 1.0 O3A B:ATP4802 3.9 50.8 1.0 NH1 B:ARG2729 4.0 91.5 1.0 CA B:SER2231 4.0 66.9 1.0 OE1 B:GLU2344 4.2 65.7 1.0 NH2 B:ARG2684 4.2 58.0 1.0 CG B:GLU2344 4.3 60.0 1.0 OD2 B:ASP2304 4.3 77.8 1.0 OE1 B:GLU2688 4.4 0.4 1.0 CD B:GLU2688 4.4 99.0 1.0 O1A B:ATP4802 4.5 54.4 1.0 PA B:ATP4802 4.5 54.1 1.0 OD1 B:ASP2304 4.5 77.1 1.0 O2A B:ATP4802 4.6 53.7 1.0 NH2 B:ARG2726 4.6 64.8 1.0 CB B:LYS2230 4.6 66.7 1.0 CE B:LYS2230 4.7 68.8 1.0 CG B:ASP2304 4.9 76.6 1.0 C B:LYS2230 4.9 61.6 1.0

K.Zhang, H.E.Foster, A.Rondelet, S.E.Lacey, N.Bahi-Buisson, A.W.Bird, A.P.Carter. Cryo-Em Reveals How Human Cytoplasmic Dynein Is Auto-Inhibited and Activated. Cell V. 169 1303 2017.
ISSN: ISSN 1097-4172
PubMed: 28602352
DOI: 10.1016/J.CELL.2017.05.025