Magnesium in PDB 3t0q: Motor Domain Structure of the KAR3-Like Kinesin From Ashbya Gossypii

The structure of Motor Domain Structure of the KAR3-Like Kinesin From Ashbya Gossypii, PDB code: 3t0q was solved by D.Duan, D.J.Hnatchuk, J.Brenner, D.Davis, J.S.Allingham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.64 / 2.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.866, 84.623, 101.141, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 25.3

The binding sites of Magnesium atom in the Motor Domain Structure of the KAR3-Like Kinesin From Ashbya Gossypii (pdb code 3t0q). 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 Motor Domain Structure of the KAR3-Like Kinesin From Ashbya Gossypii, PDB code: 3t0q:

Magnesium binding site 1 out of 1 in the Motor Domain Structure of the KAR3-Like Kinesin From Ashbya Gossypii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Motor Domain Structure of the KAR3-Like Kinesin From Ashbya Gossypii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg997 b:27.7 occ:1.00 O A:HOH18 2.3 27.6 1.0 O A:HOH91 2.3 33.1 1.0 OG1 A:THR460 2.3 27.2 1.0 O A:HOH17 2.3 28.3 1.0 O A:HOH16 2.4 25.6 1.0 O2B A:ADP999 2.4 21.7 1.0 O3B A:ADP999 3.2 23.9 1.0 PB A:ADP999 3.3 20.9 1.0 CB A:THR460 3.4 27.5 1.0 O A:HOH90 4.1 29.1 1.0 O2A A:ADP999 4.2 25.9 1.0 N A:THR460 4.2 24.4 1.0 OD2 A:ASP607 4.3 35.4 1.0 O3A A:ADP999 4.3 26.4 1.0 O A:HOH39 4.4 35.4 1.0 CG2 A:THR460 4.4 18.8 1.0 CA A:THR460 4.4 23.7 1.0 O A:HOH19 4.5 25.7 1.0 OD1 A:ASP607 4.5 26.8 1.0 O1B A:ADP999 4.5 22.3 1.0 PA A:ADP999 4.6 21.7 1.0 O1A A:ADP999 4.8 23.8 1.0 O A:HOH57 4.8 39.9 1.0 CG A:ASP607 4.9 30.0 1.0 CE A:LYS459 5.0 20.6 1.0

D.Duan, D.J.Hnatchuk, J.Brenner, D.Davis, J.S.Allingham. Crystal Structure of the KAR3-Like Kinesin Motor Domain From the Filamentous Fungus Ashbya Gossypii. Proteins V. 80 1016 2012.
ISSN: ISSN 0887-3585
PubMed: 22493778
DOI: 10.1002/PROT.24004