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Magnesium in PDB 1w9k: Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx

Enzymatic activity of Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx

All present enzymatic activity of Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx:
3.6.4.1;

Protein crystallography data

The structure of Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx, PDB code: 1w9k was solved by C.A.Morris, P.-D.Coureux, A.L.Wells, A.Houdusse, H.L.Sweeney, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.05
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 104.704, 179.428, 54.153, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 23.2

Other elements in 1w9k:

The structure of Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx (pdb code 1w9k). 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 Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx, PDB code: 1w9k:

Magnesium binding site 1 out of 1 in 1w9k

Go back to Magnesium Binding Sites List in 1w9k
Magnesium binding site 1 out of 1 in the Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dictyostelium Discoideum Myosin II Motor Domain S456E with Bound Mgadp-Befx within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1755

b:20.8
occ:1.00
 F2 A:BEF1757 2.0 21.2 1.0
O A:HOH2252 2.1 16.7 1.0
O2B A:ADP1756 2.1 17.1 1.0
OG1 A:THR186 2.1 16.8 1.0
OG A:SER237 2.2 19.0 1.0
O A:HOH2426 2.2 20.0 1.0
CB A:SER237 3.1 20.2 1.0
CB A:THR186 3.1 18.3 1.0
BE A:BEF1757 3.2 21.6 1.0
PB A:ADP1756 3.2 16.2 1.0
O1B A:ADP1756 3.4 17.3 1.0
N A:SER237 3.7 19.0 1.0
F3 A:BEF1757 4.0 17.5 1.0
CA A:SER237 4.0 20.5 1.0
N A:THR186 4.0 16.9 1.0
O2A A:ADP1756 4.1 18.2 1.0
CG2 A:THR186 4.1 18.2 1.0
CA A:THR186 4.1 17.2 1.0
O3A A:ADP1756 4.2 17.7 1.0
OD2 A:ASP454 4.3 21.8 1.0
F1 A:BEF1757 4.3 19.8 1.0
OD1 A:ASP454 4.3 21.1 1.0
O A:HOH2156 4.4 22.4 1.0
O A:HOH2251 4.4 31.8 1.0
O3B A:ADP1756 4.5 15.5 1.0
PA A:ADP1756 4.5 16.8 1.0
O A:ASN235 4.7 22.6 1.0
CG A:ASP454 4.7 21.5 1.0
O1A A:ADP1756 4.8 15.9 1.0
CE A:LYS185 4.8 19.0 1.0
C A:SER236 4.8 16.6 1.0
ND2 A:ASN233 4.8 16.6 1.0
CB A:LYS185 4.9 17.9 1.0
O A:HOH2157 4.9 43.8 1.0

Reference:

C.A.Morris, P.-D.Coureux, A.L.Wells, A.Houdusse, H.L.Sweeney. Structure-Function Analysis of Myosin II Backdoor Mutants To Be Published.
Page generated: Mon Dec 14 07:01:51 2020

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