Atomistry » Magnesium » PDB 4b2p-4be0 » 4bbg
Atomistry »
  Magnesium »
    PDB 4b2p-4be0 »
      4bbg »

Magnesium in PDB 4bbg: Crystal Structure of Human Kinesin EG5 in Complex with 3-(((2-Aminoethyl)Sulfanyl)(3-Ethylphenyl) Phenylmethyl)Phenol

Protein crystallography data

The structure of Crystal Structure of Human Kinesin EG5 in Complex with 3-(((2-Aminoethyl)Sulfanyl)(3-Ethylphenyl) Phenylmethyl)Phenol, PDB code: 4bbg was solved by H.Y.K.Kaan, F.Kozielski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.75
Space group I 21 3
Cell size a, b, c (Å), α, β, γ (°) 158.190, 158.190, 158.190, 90.00, 90.00, 90.00
R / Rfree (%) 18.248 / 22.964

Other elements in 4bbg:

The structure of Crystal Structure of Human Kinesin EG5 in Complex with 3-(((2-Aminoethyl)Sulfanyl)(3-Ethylphenyl) Phenylmethyl)Phenol also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Kinesin EG5 in Complex with 3-(((2-Aminoethyl)Sulfanyl)(3-Ethylphenyl) Phenylmethyl)Phenol (pdb code 4bbg). 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 EG5 in Complex with 3-(((2-Aminoethyl)Sulfanyl)(3-Ethylphenyl) Phenylmethyl)Phenol, PDB code: 4bbg:

Magnesium binding site 1 out of 1 in 4bbg

Go back to Magnesium Binding Sites List in 4bbg
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Kinesin EG5 in Complex with 3-(((2-Aminoethyl)Sulfanyl)(3-Ethylphenyl) Phenylmethyl)Phenol


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 EG5 in Complex with 3-(((2-Aminoethyl)Sulfanyl)(3-Ethylphenyl) Phenylmethyl)Phenol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:43.5
occ:1.00
O A:HOH2034 1.9 28.2 1.0
O A:HOH2033 1.9 29.8 1.0
O A:HOH2035 1.9 33.1 1.0
O A:HOH2092 2.0 34.2 1.0
O3B A:ADP600 2.0 42.0 1.0
OG1 A:THR112 2.3 39.4 1.0
CB A:THR112 3.3 39.6 1.0
PB A:ADP600 3.3 42.7 1.0
O1B A:ADP600 3.6 36.8 1.0
O2A A:ADP600 3.9 44.0 1.0
N A:THR112 4.2 40.4 1.0
OD2 A:ASP265 4.2 47.8 1.0
CA A:THR112 4.3 39.8 1.0
CG2 A:THR112 4.3 36.9 1.0
O A:SER232 4.3 48.7 1.0
O2B A:ADP600 4.3 39.9 1.0
O3A A:ADP600 4.4 43.0 1.0
OG A:SER232 4.4 52.8 1.0
OD1 A:ASP265 4.4 49.3 1.0
PA A:ADP600 4.5 43.8 1.0
O1A A:ADP600 4.6 47.2 1.0
O A:HOH2032 4.7 39.9 1.0
O A:HOH2018 4.7 58.3 1.0
CG A:ASP265 4.8 45.8 1.0
NZ A:LYS111 4.9 23.7 1.0
O A:HOH2074 4.9 48.5 1.0

Reference:

J.A.D.Good, F.Wang, O.Rath, H.Y.K.Kaan, S.K.Talapatra, D.Podgorski, S.P.Mackay, F.Kozielski. Optimized S-Trityl-L-Cysteine-Based Inhibitors of Kinesin Spindle Protein with Potent in Vivo Antitumor Activity in Lung Cancer Xenograft Models. J.Med.Chem. V. 56 1878 2013.
ISSN: ISSN 0022-2623
PubMed: 23394180
DOI: 10.1021/JM3014597
Page generated: Mon Dec 14 09:11:27 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy