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Vanadium in PDB 2jhr: Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Pentabromopseudilin

Protein crystallography data

The structure of Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Pentabromopseudilin, PDB code: 2jhr was solved by R.Fedorov, M.Boehl, G.Tsiavaliaris, F.K.Hartmann, P.Baruch, B.Brenner, R.Martin, H.J.Knoelker, H.O.Gutzeit, D.J.Manstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 89.758, 150.464, 154.550, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 26.5

Other elements in 2jhr:

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

Bromine (Br) 5 atoms
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 Pentabromopseudilin (pdb code 2jhr). 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 Pentabromopseudilin, PDB code: 2jhr:

Vanadium binding site 1 out of 1 in 2jhr

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


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 Pentabromopseudilin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V1778

b:21.2
occ:1.00
VG A:AD91778 0.0 21.2 1.0
O1G A:AD91778 1.6 13.1 1.0
O2G A:AD91778 1.7 36.7 1.0
O3G A:AD91778 1.8 31.4 1.0
O3B A:AD91778 1.8 29.4 1.0
PB A:AD91778 3.4 28.6 1.0
MG A:MG1779 3.6 31.2 1.0
N A:SER237 3.7 28.8 1.0
OG A:SER181 3.9 12.7 1.0
N A:GLY182 4.0 29.2 1.0
OG A:SER236 4.0 31.6 1.0
O A:HOH2170 4.1 9.8 1.0
ND2 A:ASN233 4.1 26.5 1.0
O2B A:AD91778 4.1 17.1 1.0
N A:GLY457 4.2 13.9 1.0
CA A:SER181 4.2 15.0 1.0
CA A:SER236 4.2 28.9 1.0
O A:HOH2307 4.2 10.6 1.0
O1B A:AD91778 4.3 27.7 1.0
O3A A:AD91778 4.3 21.8 1.0
CB A:SER181 4.5 11.9 1.0
NZ A:LYS185 4.5 25.6 1.0
C A:SER236 4.5 29.7 1.0
C A:SER181 4.6 24.8 1.0
CB A:SER237 4.6 32.2 1.0
CB A:SER236 4.6 30.1 1.0
CA A:SER237 4.7 26.8 1.0
O A:SER237 4.7 18.6 1.0
OG A:SER237 4.8 34.1 1.0
CA A:SER456 4.8 19.5 1.0
CA A:GLY457 5.0 14.6 1.0
CA A:GLY182 5.0 26.6 1.0
CE A:LYS185 5.0 23.7 1.0

Reference:

R.Fedorov, M.Bohl, G.Tsiavaliaris, F.K.Hartmann, M.H.Taft, P.Baruch, B.Brenner, R.Martin, H.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: Thu Oct 29 07:04:49 2020

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