Magnesium in PDB 9l7e: Crystal Structure of Human Kinesin-1 Motor Domain (G234A Mutant) in Complex with Adp

The structure of Crystal Structure of Human Kinesin-1 Motor Domain (G234A Mutant) in Complex with Adp, PDB code: 9l7e was solved by T.Makino, K.Miyazono, M.Tanokura, M.Tomishige, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.55 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.36, 67.93, 55.45, 90, 96.05, 90
R / Rfree (%)	19.2 / 25.2

The binding sites of Magnesium atom in the Crystal Structure of Human Kinesin-1 Motor Domain (G234A Mutant) in Complex with Adp (pdb code 9l7e). 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 Crystal Structure of Human Kinesin-1 Motor Domain (G234A Mutant) in Complex with Adp, PDB code: 9l7e:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human Kinesin-1 Motor Domain (G234A Mutant) in Complex with Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human Kinesin-1 Motor Domain (G234A Mutant) in Complex with Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:27.4 occ:1.00 O A:HOH503 2.0 22.1 1.0 OG1 A:THR92 2.1 26.1 1.0 O A:HOH506 2.2 13.6 1.0 O A:HOH504 2.2 25.2 1.0 O2B A:ADP402 2.2 27.3 1.0 CB A:THR92 3.2 29.7 1.0 PB A:ADP402 3.4 28.2 1.0 O3B A:ADP402 3.7 25.9 1.0 OD2 A:ASP231 4.0 33.9 1.0 O A:HOH513 4.1 25.8 1.0 N A:THR92 4.1 29.9 1.0 CG2 A:THR92 4.2 21.9 1.0 CA A:THR92 4.2 28.0 1.0 O2A A:ADP402 4.2 26.4 1.0 OD1 A:ASP231 4.3 29.7 1.0 O3A A:ADP402 4.4 21.9 1.0 O A:HOH538 4.4 32.5 1.0 PA A:ADP402 4.6 27.1 1.0 O1B A:ADP402 4.6 28.0 1.0 CG A:ASP231 4.6 30.4 1.0 O1A A:ADP402 4.8 27.0 1.0 CB A:LYS91 4.9 30.8 1.0 O A:HOH543 5.0 42.2 1.0

T.Makino, R.Kanada, T.Mori, K.I.Miyazono, Y.Komori, H.Yanagisawa, S.Takada, M.Tanokura, M.Kikkawa, M.Tomishige. Tension-Induced Suppression of Allosteric Conformational Changes Coordinates Kinesin-1 Stepping Biorxiv 2024.
ISSN: ISSN 2692-8205
DOI: 10.1101/2024.09.19.613825