Magnesium in PDB 2wog: Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine

The structure of Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine, PDB code: 2wog was solved by H.Y.K.Kaan, V.Ulaganathan, D.D.Hackney, F.Kozielski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.16 / 2.00
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	96.500, 96.500, 124.441, 90.00, 90.00, 120.00
R / Rfree (%)	15.5 / 21.8

The binding sites of Magnesium atom in the Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine (pdb code 2wog). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine, PDB code: 2wog:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:21.3 occ:1.00 OG1 A:THR112 2.0 19.9 1.0 O A:HOH2237 2.1 19.0 1.0 O A:HOH2103 2.1 20.7 1.0 O1B A:ADP600 2.1 18.3 1.0 O A:HOH2303 2.2 21.2 1.0 O A:HOH2298 2.8 19.1 1.0 CB A:THR112 3.1 19.7 1.0 PB A:ADP600 3.3 20.1 1.0 O3B A:ADP600 3.5 15.4 1.0 N A:THR112 3.9 18.6 1.0 CA A:THR112 4.1 18.7 1.0 OD2 A:ASP265 4.1 30.4 1.0 O A:HOH2238 4.1 19.9 1.0 CG2 A:THR112 4.2 22.7 1.0 O A:HOH2216 4.2 30.5 1.0 O A:HOH2204 4.3 33.5 1.0 OD1 A:ASP265 4.3 25.1 1.0 O1A A:ADP600 4.3 24.6 1.0 O A:HOH2099 4.3 17.1 1.0 O A:HOH2203 4.3 35.2 1.0 O2B A:ADP600 4.4 21.0 1.0 O3A A:ADP600 4.4 19.8 1.0 O A:SER232 4.5 28.5 1.0 PA A:ADP600 4.6 21.6 1.0 CG A:ASP265 4.6 25.1 1.0 O2A A:ADP600 4.7 23.0 1.0 O A:HOH2236 4.7 24.8 1.0 O A:HOH2215 4.9 15.4 1.0 CB A:LYS111 4.9 16.1 1.0

Magnesium binding site 2 out of 3 in the Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:20.2 occ:1.00 O B:HOH2105 1.9 20.4 1.0 O1B B:ADP600 2.1 20.1 1.0 O B:HOH2311 2.1 15.4 1.0 O B:HOH2305 2.1 16.5 1.0 OG1 B:THR112 2.2 20.4 1.0 O B:HOH2226 2.2 21.3 1.0 CB B:THR112 3.2 19.6 1.0 PB B:ADP600 3.2 18.3 1.0 O3B B:ADP600 3.4 16.9 1.0 N B:THR112 3.9 18.5 1.0 O B:HOH2228 4.0 27.5 1.0 O1A B:ADP600 4.1 21.7 1.0 CA B:THR112 4.1 18.8 1.0 O B:HOH2246 4.1 18.6 1.0 OD2 B:ASP265 4.2 23.7 1.0 O2B B:ADP600 4.3 17.4 1.0 O3A B:ADP600 4.3 17.8 1.0 CG2 B:THR112 4.3 19.2 1.0 O B:HOH2101 4.3 15.7 1.0 OD1 B:ASP265 4.4 25.0 1.0 OG B:SER232 4.4 36.2 1.0 O B:HOH2318 4.5 33.2 1.0 PA B:ADP600 4.5 21.9 1.0 O B:SER232 4.5 25.1 1.0 O B:HOH2213 4.6 30.9 1.0 O2A B:ADP600 4.6 22.8 1.0 CG B:ASP265 4.7 25.2 1.0 CB B:LYS111 4.9 16.0 1.0 O B:HOH2306 4.9 21.8 1.0 O B:HOH2244 4.9 25.8 1.0 NZ B:LYS111 4.9 18.8 1.0 O B:HOH2232 4.9 14.0 1.0 CE B:LYS111 5.0 18.9 1.0 C B:LYS111 5.0 17.9 1.0 O B:HOH2227 5.0 60.4 1.0

Magnesium binding site 3 out of 3 in the Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Intermediate and Final States of Human Kinesin EG5 in Complex with S- Trityl-L-Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:31.7 occ:1.00 O C:HOH2206 2.1 26.3 1.0 O C:HOH2074 2.1 29.3 1.0 O1B C:ADP600 2.1 24.5 1.0 O C:HOH2204 2.1 21.3 1.0 O C:HOH2168 2.1 28.0 1.0 OG1 C:THR112 2.2 27.0 1.0 CB C:THR112 3.2 28.0 1.0 PB C:ADP600 3.3 25.1 1.0 O3B C:ADP600 3.5 24.5 1.0 O C:HOH2147 3.9 37.7 1.0 N C:THR112 4.0 27.7 1.0 OD2 C:ASP265 4.1 29.2 1.0 CA C:THR112 4.1 27.8 1.0 O1A C:ADP600 4.2 32.3 1.0 O C:HOH2170 4.2 22.7 1.0 CG2 C:THR112 4.2 28.6 1.0 O C:HOH2071 4.3 23.9 1.0 O C:HOH2134 4.3 42.1 1.0 O3A C:ADP600 4.3 24.0 1.0 OD1 C:ASP265 4.4 25.7 1.0 O2B C:ADP600 4.4 24.2 1.0 O C:SER232 4.4 30.7 1.0 O C:HOH2132 4.5 44.4 1.0 PA C:ADP600 4.5 28.6 1.0 O2A C:ADP600 4.7 31.6 1.0 CG C:ASP265 4.7 26.8 1.0 O C:HOH2211 4.8 40.8 1.0 O C:HOH2169 4.8 29.5 1.0 O C:HOH2205 4.9 28.9 1.0 CB C:LYS111 4.9 25.6 1.0 NZ C:LYS111 5.0 20.9 1.0 O C:HOH2152 5.0 19.3 1.0

H.Y.K.Kaan, V.Ulaganathan, D.D.Hackney, F.Kozielski. An Allosteric Transition Trapped in An Intermediate State of A New Kinesin-Inhibitor Complex. Biochem.J. V. 425 55 2010.
ISSN: ISSN 0264-6021
PubMed: 19793049
DOI: 10.1042/BJ20091207