Magnesium in PDB 5m5l: Pseudo-Atomic Model of Microtubule-Bound S. Pombe Kinesin-5 Motor Domain in the Amppnp State (Based on Cryo-Electron Microscopy Experiment): the N-Terminus Adopts Multiple Conformations

The binding sites of Magnesium atom in the Pseudo-Atomic Model of Microtubule-Bound S. Pombe Kinesin-5 Motor Domain in the Amppnp State (Based on Cryo-Electron Microscopy Experiment): the N-Terminus Adopts Multiple Conformations (pdb code 5m5l). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Pseudo-Atomic Model of Microtubule-Bound S. Pombe Kinesin-5 Motor Domain in the Amppnp State (Based on Cryo-Electron Microscopy Experiment): the N-Terminus Adopts Multiple Conformations, PDB code: 5m5l:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Pseudo-Atomic Model of Microtubule-Bound S. Pombe Kinesin-5 Motor Domain in the Amppnp State (Based on Cryo-Electron Microscopy Experiment): the N-Terminus Adopts Multiple Conformations


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Pseudo-Atomic Model of Microtubule-Bound S. Pombe Kinesin-5 Motor Domain in the Amppnp State (Based on Cryo-Electron Microscopy Experiment): the N-Terminus Adopts Multiple Conformations within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:18.6 occ:1.00 O3G A:GTP502 2.4 28.7 1.0 O2B A:GTP502 3.2 41.2 1.0 PG A:GTP502 3.7 30.0 1.0 O3B A:GTP502 3.7 35.2 1.0 PB A:GTP502 3.8 41.4 1.0 O3A A:GTP502 4.1 39.2 1.0 O1A A:GTP502 4.4 44.5 1.0 O2G A:GTP502 4.5 35.0 1.0 PA A:GTP502 4.8 41.3 1.0 O1G A:GTP502 4.9 32.1 1.0

Magnesium binding site 2 out of 2 in the Pseudo-Atomic Model of Microtubule-Bound S. Pombe Kinesin-5 Motor Domain in the Amppnp State (Based on Cryo-Electron Microscopy Experiment): the N-Terminus Adopts Multiple Conformations


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Pseudo-Atomic Model of Microtubule-Bound S. Pombe Kinesin-5 Motor Domain in the Amppnp State (Based on Cryo-Electron Microscopy Experiment): the N-Terminus Adopts Multiple Conformations within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg501 b:31.4 occ:1.00 O2B C:ANP502 2.1 19.7 1.0 O3G C:ANP502 2.4 23.0 1.0 CA C:SER282 3.4 92.4 1.0 PB C:ANP502 3.5 21.0 1.0 PG C:ANP502 3.6 20.4 1.0 N3B C:ANP502 3.9 20.7 1.0 O2G C:ANP502 4.2 25.9 1.0 O1B C:ANP502 4.3 15.2 1.0 CA C:SER283 4.5 38.4 1.0 O3A C:ANP502 4.6 23.4 1.0 CA C:THR166 4.6 0.8 1.0 O2A C:ANP502 4.6 25.9 1.0 O1G C:ANP502 4.9 26.8 1.0 PA C:ANP502 4.9 21.4 1.0 CA C:ALA329 5.0 31.3 1.0

M.Britto, A.Goulet, S.Rizvi, O.Von Loeffelholz, C.A.Moores, R.A.Cross. Schizosaccharomyces Pombe Kinesin-5 Switches Direction Using A Steric Blocking Mechanism. Proc. Natl. Acad. Sci. V. 113 E7483 2016U.S.A..
ISSN: ESSN 1091-6490
PubMed: 27834216
DOI: 10.1073/PNAS.1611581113