Vanadium in PDB 5i0i: Crystal Structure of Myosin X Motor Domain with 2IQ Motifs in Pre- Powerstroke State

The structure of Crystal Structure of Myosin X Motor Domain with 2IQ Motifs in Pre- Powerstroke State, PDB code: 5i0i was solved by T.Isabet, H.L.Sweeney, A.Houdusse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.53 / 3.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	113.950, 173.410, 178.750, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 21.9

The structure of Crystal Structure of Myosin X Motor Domain with 2IQ Motifs in Pre- Powerstroke State also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Vanadium atom in the Crystal Structure of Myosin X Motor Domain with 2IQ Motifs in Pre- Powerstroke State (pdb code 5i0i). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Crystal Structure of Myosin X Motor Domain with 2IQ Motifs in Pre- Powerstroke State, PDB code: 5i0i:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in the Crystal Structure of Myosin X Motor Domain with 2IQ Motifs in Pre- Powerstroke State


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 X Motor Domain with 2IQ Motifs in Pre- Powerstroke State within 5.0Å range: probe atom residue distance (Å) B Occ A:V903 b:77.1 occ:1.00 V A:VO4903 0.0 77.1 1.0 O1 A:VO4903 1.6 77.4 1.0 O3 A:VO4903 1.6 75.6 1.0 O2 A:VO4903 1.6 72.3 1.0 O4 A:VO4903 1.6 75.2 1.0 O3B A:ADP904 2.4 78.5 1.0 MG A:MG902 3.4 69.4 1.0 PB A:ADP904 3.5 79.3 1.0 N A:SER219 3.7 66.8 1.0 O1B A:ADP904 3.7 79.8 1.0 OG A:SER218 3.8 83.8 1.0 OG A:SER159 3.8 92.3 1.0 CA A:SER159 3.9 66.5 1.0 N A:GLY437 3.9 78.9 1.0 ND2 A:ASN215 4.0 75.0 1.0 N A:GLY160 4.1 65.3 1.0 O A:HOH1001 4.1 71.5 1.0 CA A:SER218 4.2 64.0 1.0 CB A:SER159 4.2 71.5 1.0 NZ A:LYS163 4.2 82.2 1.0 O A:HOH1006 4.2 72.9 1.0 CB A:SER219 4.4 67.8 1.0 O3A A:ADP904 4.4 74.2 1.0 C A:SER218 4.4 70.8 1.0 O A:SER219 4.4 68.0 1.0 O2B A:ADP904 4.5 78.2 1.0 CB A:SER218 4.5 66.4 1.0 C A:SER159 4.5 68.1 1.0 OG A:SER219 4.5 73.6 1.0 CA A:SER219 4.6 65.0 1.0 CA A:GLY437 4.6 76.5 1.0 CA A:PHE436 4.7 75.8 1.0 CE A:LYS163 4.7 84.7 1.0 C A:PHE436 4.8 84.0 1.0 N A:SER159 4.9 67.7 1.0 CG A:ASN215 5.0 85.2 1.0 C A:SER219 5.0 68.7 1.0

Vanadium binding site 2 out of 2 in the Crystal Structure of Myosin X Motor Domain with 2IQ Motifs in Pre- Powerstroke State


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Crystal Structure of Myosin X Motor Domain with 2IQ Motifs in Pre- Powerstroke State within 5.0Å range: probe atom residue distance (Å) B Occ B:V904 b:0.6 occ:1.00 V B:VO4904 0.0 0.6 1.0 O3 B:VO4904 1.6 0.3 1.0 O1 B:VO4904 1.6 0.4 1.0 O2 B:VO4904 1.6 0.2 1.0 O4 B:VO4904 1.6 0.3 1.0 O3B B:ADP903 2.5 0.7 1.0 MG B:MG902 3.5 0.6 1.0 PB B:ADP903 3.7 0.0 1.0 OG B:SER218 3.7 0.7 1.0 N B:GLY437 3.8 0.8 1.0 CA B:SER159 3.9 99.4 1.0 O2B B:ADP903 3.9 0.8 1.0 N B:GLY160 3.9 0.9 1.0 N B:SER219 4.0 0.1 1.0 O B:HOH1003 4.0 1.0 1.0 ND2 B:ASN215 4.0 0.1 1.0 OG B:SER159 4.1 0.6 1.0 O B:HOH1001 4.2 80.1 1.0 NZ B:LYS163 4.3 0.2 1.0 CA B:SER218 4.3 0.3 1.0 O1B B:ADP903 4.4 0.8 1.0 O B:SER219 4.4 0.1 1.0 C B:SER159 4.4 0.5 1.0 CB B:SER159 4.4 0.9 1.0 CA B:GLY437 4.4 0.0 1.0 CB B:SER218 4.5 0.7 1.0 C B:SER218 4.6 0.3 1.0 CA B:PHE436 4.7 0.7 1.0 C B:PHE436 4.7 0.2 1.0 CE B:LYS163 4.7 0.3 1.0 CB B:SER219 4.8 0.2 1.0 O3A B:ADP903 4.8 0.1 1.0 OG B:SER219 4.9 0.3 1.0 CA B:SER219 4.9 0.7 1.0 N B:SER159 4.9 99.4 1.0 CG B:ASN215 4.9 0.4 1.0 CB B:ASN215 5.0 0.7 1.0 CA B:GLY160 5.0 0.7 1.0

V.Ropars, Z.Yang, T.Isabet, F.Blanc, K.Zhou, T.Lin, X.Liu, P.Hissier, F.Samazan, B.Amigues, E.D.Yang, H.Park, O.Pylypenko, M.Cecchini, C.V.Sindelar, H.L.Sweeney, A.Houdusse. The Myosin X Motor Is Optimized For Movement on Actin Bundles. Nat Commun V. 7 12456 2016.
ISSN: ESSN 2041-1723
PubMed: 27580874
DOI: 10.1038/NCOMMS12456