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Vanadium in PDB 3mjx: Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Blebbistatin

Protein crystallography data

The structure of Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Blebbistatin, PDB code: 3mjx was solved by R.Fedorov, P.Baruch, S.Bauer, D.J.Manstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.308, 147.026, 154.594, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 22.6

Other elements in 3mjx:

The structure of Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Blebbistatin also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Blebbistatin (pdb code 3mjx). 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 Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Blebbistatin, PDB code: 3mjx:

Vanadium binding site 1 out of 1 in 3mjx

Go back to Vanadium Binding Sites List in 3mjx
Vanadium binding site 1 out of 1 in the Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Blebbistatin


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Blebbistatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V900

b:27.8
occ:1.00
VG A:AD9900 0.0 27.8 1.0
O1G A:AD9900 1.6 24.7 1.0
O2G A:AD9900 1.7 36.8 1.0
O3B A:AD9900 1.8 48.9 1.0
O3G A:AD9900 1.8 21.9 1.0
O A:HOH1310 2.4 20.9 1.0
MG A:MG901 3.2 26.0 1.0
PB A:AD9900 3.3 24.8 1.0
OG A:SER236 3.8 24.9 1.0
N A:SER237 3.8 19.1 1.0
N A:GLY182 3.9 25.1 1.0
ND2 A:ASN233 3.9 24.1 1.0
O A:HOH1156 3.9 23.6 1.0
OG A:SER181 4.0 21.7 1.0
O1B A:AD9900 4.0 22.9 1.0
CA A:SER181 4.0 18.6 1.0
O2B A:AD9900 4.0 27.6 1.0
NZ A:LYS185 4.1 22.2 1.0
N A:GLY457 4.1 21.1 1.0
O A:HOH1143 4.2 21.7 1.0
CA A:SER236 4.2 19.0 1.0
O3A A:AD9900 4.3 30.0 1.0
CB A:SER181 4.4 18.9 1.0
O A:HOH1171 4.4 25.8 1.0
O A:SER237 4.4 25.1 1.0
CB A:SER236 4.4 15.6 1.0
C A:SER181 4.5 21.0 1.0
C A:SER236 4.5 21.7 1.0
OG A:SER237 4.5 30.0 1.0
CB A:SER237 4.6 26.3 1.0
CE A:LYS185 4.7 24.7 1.0
CA A:SER237 4.8 19.4 1.0
CA A:SER456 4.8 25.3 1.0
CA A:GLY457 4.8 13.5 1.0
CA A:GLY182 4.9 20.8 1.0
CG A:ASN233 4.9 24.5 1.0
CB A:ASN233 5.0 22.3 1.0
C A:SER456 5.0 21.8 1.0

Reference:

R.Fedorov, M.Bohl, G.Tsiavaliaris, F.K.Hartmann, M.H.Taft, P.Baruch, B.Brenner, R.Martin, H.J.Knolker, H.O.Gutzeit, D.J.Manstein. The Mechanism of Pentabromopseudilin Inhibition of Myosin Motor Activity. Nat.Struct.Mol.Biol. V. 16 80 2009.
ISSN: ISSN 1545-9993
PubMed: 19122661
DOI: 10.1038/NSMB.1542
Page generated: Wed Dec 16 02:30:53 2020

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