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Magnesium 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:

Vanadium (V) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Myosin-2 Motor Domain in Complex with Adp- Metavanadate and Blebbistatin, PDB code: 3mjx:

Magnesium binding site 1 out of 1 in 3mjx

Go back to Magnesium Binding Sites List in 3mjx
Magnesium 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 Magnesium with other atoms in the Mg 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:Mg901

b:26.0
occ:1.00
O A:HOH1156 2.1 23.6 1.0
O A:HOH1171 2.1 25.8 1.0
O1B A:AD9900 2.2 22.9 1.0
OG1 A:THR186 2.2 30.8 1.0
OG A:SER237 2.2 30.0 1.0
O2G A:AD9900 2.4 36.8 1.0
O3B A:AD9900 2.5 48.9 1.0
PB A:AD9900 3.1 24.8 1.0
VG A:AD9900 3.2 27.8 1.0
CB A:SER237 3.2 26.3 1.0
CB A:THR186 3.3 30.8 1.0
N A:SER237 3.6 19.1 1.0
O2A A:AD9900 3.9 29.4 1.0
O3A A:AD9900 4.0 30.0 1.0
CA A:SER237 4.0 19.4 1.0
O1G A:AD9900 4.1 24.7 1.0
N A:THR186 4.1 21.0 1.0
OD1 A:ASP454 4.2 26.7 1.0
CA A:THR186 4.3 23.5 1.0
O2B A:AD9900 4.3 27.6 1.0
CG2 A:THR186 4.3 25.7 1.0
PA A:AD9900 4.5 24.4 1.0
O A:ASN235 4.5 25.0 1.0
OD2 A:ASP454 4.5 25.4 1.0
O3G A:AD9900 4.6 21.9 1.0
ND2 A:ASN233 4.6 24.1 1.0
C A:SER236 4.7 21.7 1.0
O A:HOH1310 4.7 20.9 1.0
O1A A:AD9900 4.7 25.1 1.0
O A:HOH1349 4.8 30.5 1.0
CG A:ASP454 4.8 31.5 1.0
O A:ILE455 4.9 30.1 1.0
CA A:SER236 4.9 19.0 1.0
ND2 A:ASN227 5.0 29.1 1.0
CE A:LYS185 5.0 24.7 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: Mon Dec 14 08:26:22 2020

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