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Magnesium in PDB 7mgm: Structure of Yeast Cytoplasmic Dynein with AAA3 Walker B Mutation Bound to LIS1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Yeast Cytoplasmic Dynein with AAA3 Walker B Mutation Bound to LIS1 (pdb code 7mgm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Yeast Cytoplasmic Dynein with AAA3 Walker B Mutation Bound to LIS1, PDB code: 7mgm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7mgm

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Magnesium binding site 1 out of 2 in the Structure of Yeast Cytoplasmic Dynein with AAA3 Walker B Mutation Bound to LIS1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Yeast Cytoplasmic Dynein with AAA3 Walker B Mutation Bound to LIS1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg4105

b:50.7
occ:1.00
O2B A:ATP4101 2.0 55.8 1.0
OG1 A:THR1803 2.0 51.8 1.0
O3G A:ATP4101 2.4 55.8 1.0
OD2 A:ASP1848 2.6 58.8 1.0
OD1 A:ASP1848 2.9 58.8 1.0
CG A:ASP1848 3.0 58.8 1.0
CB A:THR1803 3.3 51.8 1.0
PB A:ATP4101 3.4 55.8 1.0
PG A:ATP4101 3.6 55.8 1.0
O1A A:ATP4101 3.7 55.8 1.0
O3B A:ATP4101 3.8 55.8 1.0
CG2 A:THR1803 4.0 51.8 1.0
OE2 A:GLU1849 4.1 58.9 1.0
O2G A:ATP4101 4.2 55.8 1.0
N A:THR1803 4.3 51.8 1.0
NH2 A:ARG2209 4.3 53.5 1.0
CA A:THR1803 4.4 51.8 1.0
O3A A:ATP4101 4.4 55.8 1.0
O1B A:ATP4101 4.4 55.8 1.0
OG1 A:THR1897 4.5 53.1 1.0
CB A:ASP1848 4.5 58.8 1.0
PA A:ATP4101 4.6 55.8 1.0
OD2 A:ASP2171 4.6 59.1 1.0
O1G A:ATP4101 4.9 55.8 1.0
NH1 A:ARG2209 4.9 53.5 1.0

Magnesium binding site 2 out of 2 in 7mgm

Go back to Magnesium Binding Sites List in 7mgm
Magnesium binding site 2 out of 2 in the Structure of Yeast Cytoplasmic Dynein with AAA3 Walker B Mutation Bound to LIS1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Yeast Cytoplasmic Dynein with AAA3 Walker B Mutation Bound to LIS1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg4106

b:52.2
occ:1.00
O2B A:ATP4103 1.9 57.5 1.0
O2G A:ATP4103 1.9 57.5 1.0
OG1 A:THR2081 2.0 51.8 1.0
OE2 A:GLU2195 2.1 49.1 1.0
PB A:ATP4103 3.2 57.5 1.0
CD A:GLU2195 3.3 49.1 1.0
PG A:ATP4103 3.3 57.5 1.0
CB A:THR2081 3.3 51.8 1.0
O3B A:ATP4103 3.6 57.5 1.0
O3A A:ATP4103 3.7 57.5 1.0
OE1 A:GLU2195 3.9 49.1 1.0
CG2 A:THR2081 4.2 51.8 1.0
O1A A:ATP4103 4.2 57.5 1.0
N A:THR2081 4.2 51.8 1.0
O3G A:ATP4103 4.2 57.5 1.0
OE2 A:GLU2511 4.2 52.3 1.0
OD2 A:ASP2155 4.3 53.0 1.0
O1G A:ATP4103 4.3 57.5 1.0
CA A:THR2081 4.3 51.8 1.0
CG A:GLU2195 4.4 49.1 1.0
NH2 A:ARG2549 4.4 52.2 1.0
O1B A:ATP4103 4.4 57.5 1.0
PA A:ATP4103 4.6 57.5 1.0
OD1 A:ASP2155 4.8 53.0 1.0
CG A:ASP2155 4.8 53.0 1.0
OE1 A:GLU2511 4.9 52.3 1.0
CD A:GLU2511 4.9 52.3 1.0
NH2 A:ARG2552 5.0 52.2 1.0

Reference:

J.P.Gillies, J.M.Reimer, E.P.Karasmanis, I.Lahiri, Z.M.Htet, A.E.Leschziner, S.L.Reck-Peterson. Structural Basis For Cytoplasmic Dynein-1 Regulation By LIS1. Elife V. 11 2022.
ISSN: ESSN 2050-084X
PubMed: 34994688
DOI: 10.7554/ELIFE.71229
Page generated: Thu Oct 3 00:51:17 2024

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