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Magnesium in PDB 6c1h: High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing

Magnesium Binding Sites:

The binding sites of Magnesium atom in the High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing (pdb code 6c1h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing, PDB code: 6c1h:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 6c1h

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Magnesium binding site 1 out of 5 in the High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:73.5
occ:1.00
O1A A:ADP401 2.2 76.7 1.0
NE2 A:GLN137 2.3 75.2 1.0
O3B A:ADP401 2.5 76.7 1.0
O1B A:ADP401 2.7 76.7 1.0
PB A:ADP401 3.0 76.7 1.0
PA A:ADP401 3.3 76.7 1.0
O3A A:ADP401 3.5 76.7 1.0
CD A:GLN137 3.6 75.2 1.0
CA A:GLY156 3.9 79.8 1.0
O2A A:ADP401 4.1 76.7 1.0
CG2 A:VAL339 4.3 67.5 1.0
OE1 A:GLN137 4.4 75.2 1.0
O2B A:ADP401 4.5 76.7 1.0
O5' A:ADP401 4.5 76.7 1.0
CG A:GLN137 4.5 75.2 1.0
CA A:GLY13 4.6 90.4 1.0
N A:GLY302 4.6 78.0 1.0
N A:GLY156 4.7 79.8 1.0
NZ A:LYS18 4.9 73.9 1.0

Magnesium binding site 2 out of 5 in 6c1h

Go back to Magnesium Binding Sites List in 6c1h
Magnesium binding site 2 out of 5 in the High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:77.3
occ:1.00
O1A B:ADP401 2.2 77.3 1.0
NE2 B:GLN137 2.4 66.0 1.0
O3B B:ADP401 2.4 77.3 1.0
O1B B:ADP401 2.9 77.3 1.0
PB B:ADP401 3.1 77.3 1.0
PA B:ADP401 3.3 77.3 1.0
O3A B:ADP401 3.5 77.3 1.0
CD B:GLN137 3.7 66.0 1.0
CA B:GLY156 4.1 66.2 1.0
O2A B:ADP401 4.2 77.3 1.0
CG2 B:VAL339 4.2 59.9 1.0
OE1 B:GLN137 4.4 66.0 1.0
O2B B:ADP401 4.5 77.3 1.0
CG B:GLN137 4.5 66.0 1.0
CA B:GLY13 4.6 75.0 1.0
O5' B:ADP401 4.6 77.3 1.0
N B:GLY302 4.7 63.8 1.0
NZ B:LYS18 4.7 61.3 1.0
N B:GLY156 4.8 66.2 1.0

Magnesium binding site 3 out of 5 in 6c1h

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Magnesium binding site 3 out of 5 in the High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg402

b:86.5
occ:1.00
O1A C:ADP401 2.2 89.4 1.0
NE2 C:GLN137 2.3 75.1 1.0
O3B C:ADP401 2.5 89.4 1.0
O1B C:ADP401 2.8 89.4 1.0
PB C:ADP401 3.1 89.4 1.0
PA C:ADP401 3.3 89.4 1.0
O3A C:ADP401 3.5 89.4 1.0
CD C:GLN137 3.6 75.1 1.0
CA C:GLY156 4.0 71.4 1.0
O2A C:ADP401 4.2 89.4 1.0
CG2 C:VAL339 4.2 65.4 1.0
OE1 C:GLN137 4.4 75.1 1.0
CG C:GLN137 4.4 75.1 1.0
O2B C:ADP401 4.5 89.4 1.0
O5' C:ADP401 4.6 89.4 1.0
N C:GLY302 4.6 73.4 1.0
CA C:GLY13 4.7 81.4 1.0
N C:GLY156 4.7 71.4 1.0
NZ C:LYS18 4.9 66.6 1.0
CG1 C:VAL339 4.9 65.4 1.0
OD2 C:ASP154 5.0 76.3 1.0

Magnesium binding site 4 out of 5 in 6c1h

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Magnesium binding site 4 out of 5 in the High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg402

b:89.7
occ:1.00
O1A D:ADP401 2.2 89.3 1.0
NE2 D:GLN137 2.3 0.0 1.0
O3B D:ADP401 2.7 89.3 1.0
O1B D:ADP401 2.9 89.3 1.0
PB D:ADP401 3.2 89.3 1.0
PA D:ADP401 3.4 89.3 1.0
O3A D:ADP401 3.5 89.3 1.0
CA D:GLY156 3.6 93.8 1.0
CD D:GLN137 3.6 0.0 1.0
N D:GLY156 4.2 93.8 1.0
N D:GLY302 4.3 0.6 1.0
O2A D:ADP401 4.4 89.3 1.0
OE1 D:GLN137 4.4 0.0 1.0
CG2 D:VAL339 4.5 0.6 1.0
CG D:GLN137 4.5 0.0 1.0
O5' D:ADP401 4.5 89.3 1.0
O2B D:ADP401 4.7 89.3 1.0
OD2 D:ASP154 4.7 0.7 1.0
C D:GLY156 4.8 93.8 1.0
CA D:GLY302 4.9 0.6 1.0
N D:ASP157 4.9 84.3 1.0
CA D:GLY13 5.0 0.6 1.0

Magnesium binding site 5 out of 5 in 6c1h

Go back to Magnesium Binding Sites List in 6c1h
Magnesium binding site 5 out of 5 in the High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg402

b:79.8
occ:1.00
O1A E:ADP401 2.2 79.9 1.0
NE2 E:GLN137 2.3 0.7 1.0
O1B E:ADP401 2.4 79.9 1.0
O3B E:ADP401 2.4 79.9 1.0
PB E:ADP401 2.8 79.9 1.0
PA E:ADP401 3.3 79.9 1.0
O3A E:ADP401 3.3 79.9 1.0
CD E:GLN137 3.6 0.7 1.0
CA E:GLY156 3.8 0.5 1.0
O2A E:ADP401 4.2 79.9 1.0
O2B E:ADP401 4.3 79.9 1.0
CG2 E:VAL339 4.3 0.1 1.0
OE1 E:GLN137 4.4 0.7 1.0
N E:GLY302 4.5 0.4 1.0
CG E:GLN137 4.5 0.7 1.0
O5' E:ADP401 4.5 79.9 1.0
N E:GLY156 4.6 0.5 1.0
CA E:GLY13 4.8 0.2 1.0
OD2 E:ASP154 4.9 0.1 1.0
CG1 E:VAL339 5.0 0.1 1.0

Reference:

A.Mentes, A.Huehn, X.Liu, A.Zwolak, R.Dominguez, H.Shuman, E.M.Ostap, C.V.Sindelar. High-Resolution Cryo-Em Structures of Actin-Bound Myosin States Reveal the Mechanism of Myosin Force Sensing. Proc. Natl. Acad. Sci. V. 115 1292 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29358376
DOI: 10.1073/PNAS.1718316115
Page generated: Mon Sep 30 20:05:55 2024

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