Fluorine in PDB 4ck7: Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment

The structure of Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Aluminium	(Al)	1 atom

The binding sites of Fluorine atom in the Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment (pdb code 4ck7). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment, PDB code: 4ck7:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment within 5.0Å range: probe atom residue distance (Å) B Occ C:F1206 b:81.8 occ:1.00 F1 C:AF31206 0.0 81.8 1.0 AL C:AF31206 1.9 76.3 1.0 MG C:MG1205 2.1 54.4 1.0 O3B C:ADP1207 2.9 42.8 1.0 F2 C:AF31206 3.2 65.7 1.0 F3 C:AF31206 3.2 62.0 1.0 CA C:SER232 3.7 13.4 1.0 O2A C:ADP1207 3.8 51.4 1.0 PB C:ADP1207 4.3 44.1 1.0 CA C:ASN229 5.0 14.8 1.0 PA C:ADP1207 5.0 52.7 1.0

Fluorine binding site 2 out of 3 in the Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment within 5.0Å range: probe atom residue distance (Å) B Occ C:F1206 b:65.7 occ:1.00 F2 C:AF31206 0.0 65.7 1.0 AL C:AF31206 1.8 76.3 1.0 O3B C:ADP1207 2.5 42.8 1.0 F1 C:AF31206 3.2 81.8 1.0 F3 C:AF31206 3.2 62.0 1.0 PB C:ADP1207 3.7 44.1 1.0 O1B C:ADP1207 3.7 50.0 1.0 CA C:THR107 3.7 9.0 1.0 MG C:MG1205 4.2 54.4 1.0 O2B C:ADP1207 4.5 57.9 1.0 O3A C:ADP1207 4.9 50.1 1.0

Fluorine binding site 3 out of 3 in the Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in Presence of Adp.Alfx (Neck-Linker in Its Disconnected Conformation, Based on Cryo-Electron Microscopy Experiment within 5.0Å range: probe atom residue distance (Å) B Occ C:F1206 b:62.0 occ:1.00 F3 C:AF31206 0.0 62.0 1.0 AL C:AF31206 1.9 76.3 1.0 MG C:MG1205 3.0 54.4 1.0 O3B C:ADP1207 3.2 42.8 1.0 F2 C:AF31206 3.2 65.7 1.0 F1 C:AF31206 3.2 81.8 1.0 O2B C:ADP1207 4.1 57.9 1.0 PB C:ADP1207 4.2 44.1 1.0 CA C:SER232 4.3 13.4 1.0 CA C:SER233 4.5 11.7 1.0

A.Goulet, J.Major, Y.Jun, S.P.Gross, S.S.Rosenfeld, C.A.Moores. Comprehensive Structural Model of the Mechanochemical Cycle of A Mitotic Motor Highlights Molecular Adaptations in the Kinesin Family. Proc.Natl.Acad.Sci.Usa V. 111 1837 2014.
ISSN: ISSN 0027-8424
PubMed: 24449904
DOI: 10.1073/PNAS.1319848111