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Magnesium in PDB 4aqw: Model of Human Kinesin-5 Motor Domain (1II6, 3HQD) and Mammalian Tubulin Heterodimer (1JFF) Docked Into the 9.5-Angstrom Cryo-Em Map of Microtubule-Bound Kinesin-5 Motor Domain in the Rigor State.

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Model of Human Kinesin-5 Motor Domain (1II6, 3HQD) and Mammalian Tubulin Heterodimer (1JFF) Docked Into the 9.5-Angstrom Cryo-Em Map of Microtubule-Bound Kinesin-5 Motor Domain in the Rigor State. (pdb code 4aqw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Model of Human Kinesin-5 Motor Domain (1II6, 3HQD) and Mammalian Tubulin Heterodimer (1JFF) Docked Into the 9.5-Angstrom Cryo-Em Map of Microtubule-Bound Kinesin-5 Motor Domain in the Rigor State., PDB code: 4aqw:

Magnesium binding site 1 out of 1 in 4aqw

Go back to Magnesium Binding Sites List in 4aqw
Magnesium binding site 1 out of 1 in the Model of Human Kinesin-5 Motor Domain (1II6, 3HQD) and Mammalian Tubulin Heterodimer (1JFF) Docked Into the 9.5-Angstrom Cryo-Em Map of Microtubule-Bound Kinesin-5 Motor Domain in the Rigor State.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Model of Human Kinesin-5 Motor Domain (1II6, 3HQD) and Mammalian Tubulin Heterodimer (1JFF) Docked Into the 9.5-Angstrom Cryo-Em Map of Microtubule-Bound Kinesin-5 Motor Domain in the Rigor State. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:18.6
occ:1.00
O1G A:GTP500 2.4 28.7 1.0
O2B A:GTP500 3.2 41.2 1.0
PG A:GTP500 3.7 30.0 1.0
O3B A:GTP500 3.7 35.2 1.0
PB A:GTP500 3.8 41.4 1.0
CA A:GLN11 3.9 23.8 1.0
O3A A:GTP500 4.1 39.2 1.0
O1A A:GTP500 4.4 44.5 1.0
O3G A:GTP500 4.5 35.0 1.0
PA A:GTP500 4.8 41.3 1.0
O2G A:GTP500 4.9 32.1 1.0

Reference:

A.Goulet, W.M.Behnke-Parks, C.V.Sindelar, J.Major, S.S.Rosenfeld, C.Moores. The Structural Basis of Force Generation By the Mitotic Motor Kinesin-5. J.Biol.Chem. V. 287 44654 2012.
ISSN: ISSN 0021-9258
PubMed: 23135273
DOI: 10.1074/JBC.M112.404228
Page generated: Mon Dec 14 09:08:37 2020

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