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Magnesium in PDB 2xel: Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity

Protein crystallography data

The structure of Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity, PDB code: 2xel was solved by K.Chinthalapudi, M.H.Taft, R.Martin, F.K.Hartmann, S.M.Heissler, G.Tsiavaliaris, H.O.Gutzeit, H.J.Knoelker, L.M.Coluccio, R.Fedorov, D.J.Manstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.59 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.530, 147.490, 153.780, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 25.3

Other elements in 2xel:

The structure of Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms
Vanadium (V) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity (pdb code 2xel). 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 Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity, PDB code: 2xel:

Magnesium binding site 1 out of 1 in 2xel

Go back to Magnesium Binding Sites List in 2xel
Magnesium binding site 1 out of 1 in the Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg901

b:31.1
occ:1.00
O A:HOH2205 2.1 34.2 1.0
OG A:SER237 2.2 43.3 1.0
OG1 A:THR186 2.4 34.5 1.0
O3G A:AD9900 2.4 43.6 1.0
O2B A:AD9900 2.5 42.6 1.0
O3B A:AD9900 2.6 43.3 1.0
CB A:SER237 3.1 29.2 1.0
VG A:AD9900 3.2 41.9 1.0
PB A:AD9900 3.2 39.4 1.0
CB A:THR186 3.5 29.3 1.0
N A:SER237 3.7 28.5 1.0
CA A:SER237 4.0 26.2 1.0
O2G A:AD9900 4.1 39.4 1.0
OD1 A:ASP454 4.1 33.8 1.0
O2A A:AD9900 4.2 41.7 1.0
N A:THR186 4.2 18.5 1.0
O3A A:AD9900 4.3 42.6 1.0
O1B A:AD9900 4.4 41.2 1.0
CA A:THR186 4.4 22.4 1.0
O1G A:AD9900 4.6 42.9 1.0
OD2 A:ASP454 4.6 29.3 1.0
O A:ILE455 4.6 44.6 1.0
CG2 A:THR186 4.6 25.8 1.0
O A:HOH2309 4.7 41.4 1.0
CE A:LYS185 4.7 22.1 1.0
O A:ASN235 4.7 24.9 1.0
PA A:AD9900 4.7 38.0 1.0
O A:HOH2194 4.8 50.0 1.0
CG A:ASP454 4.8 28.7 1.0
ND2 A:ASN233 4.8 30.2 1.0
C A:SER236 4.9 26.1 1.0
O A:SER237 4.9 30.4 1.0

Reference:

K.Chinthalapudi, M.H.Taft, R.Martin, S.M.Heissler, M.Preller, F.K.Hartmann, H.Brandstaetter, J.Kendrick-Jones, G.Tsiavaliaris, H.O.Gutzeit, R.Fedorov, F.Buss, H.J.Knoelker, L.M.Coluccio, D.J.Manstein. Mechanism and Specificity of Pentachloropseudilin- Mediated Inhibition of Myosin Motor Activity. J.Biol.Chem. V. 286 29700 2011.
ISSN: ISSN 0021-9258
PubMed: 21680745
DOI: 10.1074/JBC.M111.239210
Page generated: Mon Dec 14 07:46:33 2020

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