Manganese in PDB 3pxn: Crystal Structure of the Drosophila Kinesin Family Member KIN10/Nod in Complex with Divalent Manganese and Adp

The structure of Crystal Structure of the Drosophila Kinesin Family Member KIN10/Nod in Complex with Divalent Manganese and Adp, PDB code: 3pxn was solved by J.C.Cochran, Y.C.Zhao, D.E.Wilcox, F.J.Kull, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.69 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.557, 75.712, 94.197, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 27

The binding sites of Manganese atom in the Crystal Structure of the Drosophila Kinesin Family Member KIN10/Nod in Complex with Divalent Manganese and Adp (pdb code 3pxn). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the Drosophila Kinesin Family Member KIN10/Nod in Complex with Divalent Manganese and Adp, PDB code: 3pxn:

Manganese binding site 1 out of 1 in the Crystal Structure of the Drosophila Kinesin Family Member KIN10/Nod in Complex with Divalent Manganese and Adp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Drosophila Kinesin Family Member KIN10/Nod in Complex with Divalent Manganese and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:43.5 occ:1.00 O2B A:ADP401 2.3 35.8 1.0 OG A:SER94 2.6 29.7 1.0 CB A:SER94 3.3 28.0 1.0 PB A:ADP401 3.4 34.5 1.0 O3B A:ADP401 3.4 39.4 1.0 N A:SER94 4.0 30.9 1.0 OD2 A:ASP226 4.0 32.1 1.0 OD1 A:ASP226 4.1 31.6 1.0 O1B A:ADP401 4.1 35.0 1.0 CA A:SER94 4.2 29.7 1.0 O2A A:ADP401 4.3 38.2 1.0 CG A:ASP226 4.5 30.2 1.0 O A:HOH513 4.5 45.0 1.0 O3A A:ADP401 4.7 37.6 1.0 O1A A:ADP401 4.8 39.0 1.0 CE A:LYS93 4.9 29.8 1.0 PA A:ADP401 4.9 37.4 1.0 CB A:LYS93 5.0 26.1 1.0

J.C.Cochran, Y.C.Zhao, D.E.Wilcox, F.J.Kull. A Metal Switch For Controlling the Activity of Molecular Motor Proteins. Nat.Struct.Mol.Biol. V. 19 122 2012.
ISSN: ISSN 1545-9993
PubMed: 22198464
DOI: 10.1038/NSMB.2190