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Magnesium in PDB 1l2o: Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation

Protein crystallography data

The structure of Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation, PDB code: 1l2o was solved by M.Himmel, S.Gourinath, L.Reshetnikova, Y.Shen, G.Szent-Gyorgyi, C.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 54.16 / 2.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 51.800, 57.000, 150.500, 95.60, 96.30, 101.50
R / Rfree (%) 28 / 32.7

Other elements in 1l2o:

The structure of Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation (pdb code 1l2o). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation, PDB code: 1l2o:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1l2o

Go back to Magnesium Binding Sites List in 1l2o
Magnesium binding site 1 out of 2 in the Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg903

b:90.7
occ:1.00
O2B A:ADP999 1.9 85.6 1.0
OG1 A:THR183 2.0 64.3 1.0
O A:HOH1016 2.1 95.4 1.0
O A:HOH1017 2.1 78.8 1.0
OG A:SER241 2.4 77.2 1.0
CB A:THR183 2.7 67.5 1.0
CB A:SER241 2.8 67.4 1.0
PB A:ADP999 2.9 82.0 1.0
O3B A:ADP999 3.0 88.0 1.0
N A:SER241 3.3 65.8 1.0
CG2 A:THR183 3.6 67.3 1.0
CA A:SER241 3.7 68.2 1.0
O2A A:ADP999 3.7 83.2 1.0
O3A A:ADP999 3.8 81.2 1.0
CA A:THR183 3.9 68.3 1.0
N A:THR183 4.0 64.7 1.0
O A:HOH1022 4.0 61.1 1.0
O A:HOH1023 4.0 79.3 1.0
O1B A:ADP999 4.2 83.7 1.0
PA A:ADP999 4.2 81.4 1.0
O A:ASN239 4.4 69.2 1.0
C A:SER240 4.4 63.7 1.0
OD2 A:ASP460 4.4 16.4 1.0
O A:HOH1019 4.4 77.0 1.0
NZ A:LYS182 4.7 70.7 1.0
O1A A:ADP999 4.7 77.3 1.0
O A:SER241 4.7 69.8 1.0
CA A:SER240 4.7 64.3 1.0
C A:SER241 4.7 68.1 1.0
ND2 A:ASN237 4.8 55.5 1.0
C A:THR183 4.9 71.3 1.0
OD1 A:ASP460 4.9 11.2 1.0

Magnesium binding site 2 out of 2 in 1l2o

Go back to Magnesium Binding Sites List in 1l2o
Magnesium binding site 2 out of 2 in the Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Scallop Myosin S1-Adp-P-Pdm in the Actin-Detached Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg902

b:0.6
occ:1.00
OD1 B:ASP32 1.9 0.8 1.0
N B:ASP32 2.1 0.4 1.0
OD1 B:ASP28 2.3 0.4 1.0
OD2 B:ASP39 2.5 0.6 1.0
OD1 B:ASP30 2.5 0.6 1.0
CG B:ASP32 2.7 0.6 1.0
CG B:ASP30 2.7 0.6 1.0
N B:ARG31 2.8 0.6 1.0
CB B:ASP32 2.8 0.6 1.0
CA B:ASP32 2.9 0.5 1.0
OD2 B:ASP30 2.9 0.6 1.0
CG B:ASP28 3.1 0.4 1.0
C B:ARG31 3.1 0.0 1.0
O B:PHE34 3.1 95.0 1.0
CA B:ARG31 3.3 0.5 1.0
C B:ASP30 3.4 0.6 1.0
OD2 B:ASP28 3.4 97.6 1.0
CG B:ASP39 3.4 0.6 1.0
C B:ASP32 3.6 0.6 1.0
OD1 B:ASP39 3.7 0.5 1.0
CB B:ASP30 3.7 0.6 1.0
CA B:ASP30 3.8 0.4 1.0
OD2 B:ASP32 3.9 0.6 1.0
N B:ASP30 3.9 0.1 1.0
O B:ASP30 4.1 0.6 1.0
N B:GLY33 4.1 0.8 1.0
O B:ASP32 4.3 0.6 1.0
O B:ARG31 4.3 0.7 1.0
CB B:ASP28 4.3 0.6 1.0
C B:PHE34 4.3 97.4 1.0
C B:ASP28 4.3 0.0 1.0
CA B:ASP28 4.3 0.8 1.0
O B:ASP28 4.4 0.4 1.0
N B:PHE34 4.5 99.8 1.0
OG B:SER36 4.6 93.1 1.0
C B:VAL29 4.7 0.6 1.0
N B:VAL29 4.7 0.6 1.0
CB B:ARG31 4.7 0.7 1.0
CB B:ASP39 4.8 0.6 1.0
CA B:PHE34 5.0 98.3 1.0

Reference:

D.M.Himmel, S.Gourinath, L.Reshetnikova, Y.Shen, A.G.Szent-Gyorgyi, C.Cohen. Crystallographic Findings on the Internally Uncoupled and Near-Rigor States of Myosin: Further Insights Into the Mechanics of the Motor. Proc.Natl.Acad.Sci.Usa V. 99 12645 2002.
ISSN: ISSN 0027-8424
PubMed: 12297624
DOI: 10.1073/PNAS.202476799
Page generated: Mon Dec 14 06:22:47 2020

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