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Aluminium in PDB 4ck6: Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in the Adp.Alfx State, Based on Cryo-Electron Microscopy Experiment.

Other elements in 4ck6:

The structure of Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in the Adp.Alfx State, Based on Cryo-Electron Microscopy Experiment. also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Magnesium (Mg) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in the Adp.Alfx State, Based on Cryo-Electron Microscopy Experiment. (pdb code 4ck6). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in the Adp.Alfx State, Based on Cryo-Electron Microscopy Experiment., PDB code: 4ck6:

Aluminium binding site 1 out of 1 in 4ck6

Go back to Aluminium Binding Sites List in 4ck6
Aluminium binding site 1 out of 1 in the Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in the Adp.Alfx State, Based on Cryo-Electron Microscopy Experiment.


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Pseudo-Atomic Model of Microtubule-Bound Human Kinesin-5 Motor Domain in the Adp.Alfx State, Based on Cryo-Electron Microscopy Experiment. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Al1206

b:76.3
occ:1.00
AL C:AF31206 0.0 76.3 1.0
F2 C:AF31206 1.8 65.7 1.0
F1 C:AF31206 1.9 81.8 1.0
F3 C:AF31206 1.9 62.0 1.0
O3B C:ADP1207 2.3 42.8 1.0
MG C:MG1205 2.7 54.4 1.0
PB C:ADP1207 3.7 44.1 1.0
CA C:SER232 4.2 13.4 1.0
O2B C:ADP1207 4.3 57.9 1.0
O1B C:ADP1207 4.4 50.0 1.0
O2A C:ADP1207 4.6 51.4 1.0
O3A C:ADP1207 4.9 50.1 1.0

Reference:

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
Page generated: Sat Dec 12 01:32:55 2020

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