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Magnesium in PDB 1w9i: Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx

Enzymatic activity of Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx

All present enzymatic activity of Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx:
3.6.4.1;

Protein crystallography data

The structure of Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx, PDB code: 1w9i 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 / 1.75
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 105.017, 186.506, 54.713, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 20.7

Other elements in 1w9i:

The structure of Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx (pdb code 1w9i). 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 Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx, PDB code: 1w9i:

Magnesium binding site 1 out of 1 in 1w9i

Go back to Magnesium Binding Sites List in 1w9i
Magnesium binding site 1 out of 1 in the Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Myosin II Dictyostelium Discoideum Motor Domain S456Y Bound with Mgadp-Befx within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1755

b:10.7
occ:1.00
 F3 A:BEF1757 2.0 10.9 1.0
O2B A:ADP1756 2.1 10.2 1.0
O A:HOH2702 2.1 11.1 1.0
OG1 A:THR186 2.1 11.4 1.0
O A:HOH2451 2.2 9.4 1.0
OG A:SER237 2.2 10.7 1.0
CB A:THR186 3.1 10.8 1.0
CB A:SER237 3.2 11.2 1.0
BE A:BEF1757 3.2 12.9 1.0
PB A:ADP1756 3.3 10.1 1.0
O1B A:ADP1756 3.6 9.8 1.0
N A:SER237 3.8 11.1 1.0
N A:THR186 4.1 10.8 1.0
F2 A:BEF1757 4.1 11.8 1.0
CA A:SER237 4.1 11.1 1.0
O2A A:ADP1756 4.1 11.4 1.0
CG2 A:THR186 4.1 12.7 1.0
O A:HOH2453 4.2 42.6 1.0
CA A:THR186 4.2 11.2 1.0
OD2 A:ASP454 4.2 14.5 1.0
OD1 A:ASP454 4.3 15.4 1.0
O A:HOH2452 4.3 37.6 1.0
F1 A:BEF1757 4.3 11.6 1.0
O3A A:ADP1756 4.3 10.2 1.0
O A:HOH2286 4.4 16.4 1.0
O3B A:ADP1756 4.5 9.7 1.0
PA A:ADP1756 4.6 10.8 1.0
CG A:ASP454 4.8 13.9 1.0
O A:ASN235 4.8 12.6 1.0
O A:HOH2285 4.8 22.0 1.0
O A:HOH2294 4.8 22.6 1.0
ND2 A:ASN233 4.9 11.1 1.0
O1A A:ADP1756 4.9 12.1 1.0
C A:SER236 4.9 11.1 1.0
CE A:LYS185 4.9 10.1 1.0
CB A:LYS185 5.0 11.0 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: Sun Aug 10 06:46:28 2025

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