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Vanadium 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:

Magnesium (Mg) 1 atom
Chlorine (Cl) 5 atoms

Vanadium Binding Sites:

The binding sites of Vanadium 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 Vanadium atom.
In total only one binding site of Vanadium was determined in the Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity, PDB code: 2xel:

Vanadium binding site 1 out of 1 in 2xel

Go back to Vanadium Binding Sites List in 2xel
Vanadium 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 Vanadium with other atoms in the V 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:V900

b:41.9
occ:1.00
VG A:AD9900 0.0 41.9 1.0
O2G A:AD9900 1.6 39.4 1.0
O3G A:AD9900 1.7 43.6 1.0
O1G A:AD9900 1.8 42.9 1.0
O3B A:AD9900 1.8 43.3 1.0
MG A:MG901 3.2 31.1 1.0
PB A:AD9900 3.3 39.4 1.0
OG A:SER181 3.7 24.2 1.0
ND2 A:ASN233 3.7 30.2 1.0
N A:GLY182 3.9 31.7 1.0
CA A:SER181 4.0 26.3 1.0
OG A:SER236 4.0 23.9 1.0
N A:SER237 4.0 28.5 1.0
O1B A:AD9900 4.1 41.2 1.0
NZ A:LYS185 4.1 24.9 1.0
O2B A:AD9900 4.1 42.6 1.0
N A:GLY457 4.1 25.5 1.0
CB A:SER181 4.2 21.4 1.0
O A:HOH2205 4.2 34.2 1.0
O A:HOH2312 4.2 38.4 1.0
O3A A:AD9900 4.3 42.6 1.0
CA A:SER236 4.4 29.2 1.0
C A:SER181 4.5 28.0 1.0
OG A:SER237 4.5 43.3 1.0
CE A:LYS185 4.6 22.1 1.0
O A:SER237 4.6 30.4 1.0
CB A:SER236 4.6 27.1 1.0
CB A:SER237 4.7 29.2 1.0
C A:SER236 4.7 26.1 1.0
CG A:ASN233 4.8 20.1 1.0
CA A:SER456 4.8 28.0 1.0
CA A:GLY457 4.9 23.3 1.0
CA A:SER237 4.9 26.2 1.0
CA A:GLY182 4.9 32.2 1.0
CB A:ASN233 5.0 18.6 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: Thu Oct 29 07:04:55 2020

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