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Magnesium in PDB 5i0h: Crystal Structure of Myosin X Motor Domain in Pre-Powerstroke State

Protein crystallography data

The structure of Crystal Structure of Myosin X Motor Domain in Pre-Powerstroke State, PDB code: 5i0h was solved by T.Isabet, F.Blanc, H.L.Sweeney, A.Houdusse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.35 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 76.480, 78.300, 78.670, 75.69, 86.38, 76.12
R / Rfree (%) 16.5 / 19

Other elements in 5i0h:

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

Fluorine (F) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Myosin X Motor Domain in Pre-Powerstroke State (pdb code 5i0h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Myosin X Motor Domain in Pre-Powerstroke State, PDB code: 5i0h:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5i0h

Go back to Magnesium Binding Sites List in 5i0h
Magnesium binding site 1 out of 2 in the Crystal Structure of Myosin X Motor Domain in Pre-Powerstroke State


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 X Motor Domain in Pre-Powerstroke State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg802

b:20.4
occ:1.00
F2 A:BEF803 2.0 20.2 1.0
O A:HOH1073 2.1 16.8 1.0
OG1 A:THR164 2.1 16.5 1.0
O2B A:ADP801 2.1 17.7 1.0
OG A:SER219 2.1 18.7 1.0
O A:HOH909 2.1 16.9 1.0
CB A:THR164 3.1 18.3 1.0
CB A:SER219 3.2 18.0 1.0
BE A:BEF803 3.2 21.2 1.0
PB A:ADP801 3.3 18.9 1.0
O3B A:ADP801 3.5 17.9 1.0
N A:SER219 3.8 17.2 1.0
N A:THR164 3.9 16.4 1.0
OD1 A:ASP434 4.1 26.1 1.0
CA A:THR164 4.1 16.1 1.0
F1 A:BEF803 4.1 20.7 1.0
O2A A:ADP801 4.1 17.5 1.0
CA A:SER219 4.1 16.0 1.0
CG2 A:THR164 4.2 19.6 1.0
O3A A:ADP801 4.2 18.5 1.0
O A:HOH1028 4.3 22.9 1.0
OD2 A:ASP434 4.3 26.2 1.0
F3 A:BEF803 4.4 18.4 1.0
O1B A:ADP801 4.4 17.7 1.0
O A:ASN217 4.6 19.2 1.0
PA A:ADP801 4.6 18.2 1.0
CG A:ASP434 4.6 23.3 1.0
ND2 A:ASN215 4.7 17.2 1.0
O1A A:ADP801 4.7 19.1 1.0
O A:ILE435 4.7 21.3 1.0
C A:SER218 4.8 20.6 1.0
O A:HOH1006 4.9 24.7 1.0
CE A:LYS163 5.0 18.2 1.0
CB A:LYS163 5.0 19.1 1.0

Magnesium binding site 2 out of 2 in 5i0h

Go back to Magnesium Binding Sites List in 5i0h
Magnesium binding site 2 out of 2 in the Crystal Structure of Myosin X Motor Domain in Pre-Powerstroke State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Myosin X Motor Domain in Pre-Powerstroke State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg802

b:22.0
occ:1.00
F2 B:BEF803 2.0 19.9 1.0
O B:HOH910 2.1 19.2 1.0
OG B:SER219 2.1 21.2 1.0
O3B B:ADP801 2.1 19.1 1.0
OG1 B:THR164 2.1 19.5 1.0
O B:HOH963 2.1 19.5 1.0
CB B:THR164 3.1 21.3 1.0
CB B:SER219 3.2 20.1 1.0
BE B:BEF803 3.2 22.3 1.0
PB B:ADP801 3.3 20.6 1.0
O1B B:ADP801 3.5 22.7 1.0
N B:SER219 3.8 19.0 1.0
N B:THR164 3.9 21.1 1.0
OD1 B:ASP434 4.0 31.5 1.0
F1 B:BEF803 4.0 22.0 1.0
CA B:THR164 4.1 20.0 1.0
CA B:SER219 4.1 18.1 1.0
O1A B:ADP801 4.1 19.7 1.0
CG2 B:THR164 4.2 25.6 1.0
O3A B:ADP801 4.3 20.0 1.0
O B:HOH931 4.3 25.7 1.0
OD2 B:ASP434 4.3 28.7 1.0
O2B B:ADP801 4.4 20.0 1.0
F3 B:BEF803 4.4 22.3 1.0
PA B:ADP801 4.6 21.6 1.0
O B:ASN217 4.6 22.3 1.0
CG B:ASP434 4.6 29.9 1.0
ND2 B:ASN215 4.7 18.8 1.0
O B:ILE435 4.7 23.4 0.5
O2A B:ADP801 4.7 21.8 1.0
O B:ILE435 4.8 20.3 0.5
C B:SER218 4.8 21.8 1.0
O B:HOH1002 4.9 24.6 1.0
CE B:LYS163 4.9 19.2 1.0
CB B:LYS163 5.0 21.0 1.0
C B:LYS163 5.0 22.9 1.0

Reference:

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
Page generated: Sun Sep 29 16:37:53 2024

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