Magnesium in PDB 1yv3: The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II

The structure of The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II, PDB code: 1yv3 was solved by J.S.Allingham, R.Smith, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	88.106, 145.770, 152.912, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 21.5

The structure of The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II also contains other interesting chemical elements:

Vanadium

(V)

1 atom

The binding sites of Magnesium atom in the The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II (pdb code 1yv3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II, PDB code: 1yv3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg997 b:10.7 occ:1.00 O1 A:VO4998 2.0 11.8 1.0 O A:HOH1454 2.0 11.8 1.0 O1B A:ADP1000 2.1 11.1 1.0 O A:HOH1276 2.1 10.5 1.0 OG1 A:THR186 2.1 11.6 1.0 OG A:SER237 2.2 9.6 1.0 CB A:THR186 3.1 12.9 1.0 CB A:SER237 3.1 11.5 1.0 PB A:ADP1000 3.2 11.1 1.0 V A:VO4998 3.5 10.2 1.0 O3B A:ADP1000 3.6 10.3 1.0 N A:SER237 3.8 11.9 1.0 N A:THR186 4.0 11.6 1.0 CA A:SER237 4.0 10.6 1.0 CG2 A:THR186 4.0 16.5 1.0 O2A A:ADP1000 4.1 11.7 1.0 OD1 A:ASP454 4.1 17.2 1.0 CA A:THR186 4.1 12.3 1.0 OD2 A:ASP454 4.1 15.3 1.0 O3A A:ADP1000 4.3 9.2 1.0 O3 A:VO4998 4.4 11.2 1.0 O2B A:ADP1000 4.4 11.2 1.0 O A:HOH1043 4.5 19.3 1.0 O4 A:VO4998 4.5 12.0 1.0 PA A:ADP1000 4.5 11.3 1.0 CG A:ASP454 4.6 14.2 1.0 O A:ASN235 4.6 11.6 1.0 O1A A:ADP1000 4.7 10.2 1.0 O2 A:VO4998 4.8 9.2 1.0 O A:ILE455 4.9 13.0 1.0 C A:SER236 4.9 11.6 1.0 ND2 A:ASN233 4.9 9.5 1.0 ND2 A:ASN227 5.0 11.0 1.0

Magnesium binding site 2 out of 2 in the The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg999 b:24.1 occ:0.50 O A:HOH1115 1.7 29.0 1.0 O A:HOH1547 2.1 34.0 1.0 O A:HOH1114 2.1 24.4 1.0 OE2 A:GLU567 3.3 35.2 1.0 OE1 A:GLU567 3.8 32.4 1.0 CD A:GLU567 3.9 29.7 1.0 O A:LYS462 4.3 18.3 1.0 CE1 A:PHE563 4.8 15.2 1.0 O A:HOH1376 5.0 32.1 1.0 O A:HOH1085 5.0 19.3 1.0

J.S.Allingham, R.Smith, I.Rayment. The Structural Basis of Blebbistatin Inhibition and Specificity For Myosin II. Nat.Struct.Mol.Biol. V. 12 378 2005.
ISSN: ISSN 1545-9993
PubMed: 15750603
DOI: 10.1038/NSMB908