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Magnesium in PDB 8fo2: Cryo-Em Structure of RAB29-LRRK2 Complex in the LRRK2 Monomer State

Enzymatic activity of Cryo-Em Structure of RAB29-LRRK2 Complex in the LRRK2 Monomer State

All present enzymatic activity of Cryo-Em Structure of RAB29-LRRK2 Complex in the LRRK2 Monomer State:
2.7.11.1;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of RAB29-LRRK2 Complex in the LRRK2 Monomer State (pdb code 8fo2). 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 Cryo-Em Structure of RAB29-LRRK2 Complex in the LRRK2 Monomer State, PDB code: 8fo2:

Magnesium binding site 1 out of 1 in 8fo2

Go back to Magnesium Binding Sites List in 8fo2
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of RAB29-LRRK2 Complex in the LRRK2 Monomer State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of RAB29-LRRK2 Complex in the LRRK2 Monomer State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg201

b:30.0
occ:1.00
O2B B:GNP202 1.7 5.7 1.0
O3G B:GNP202 1.9 8.5 1.0
OG1 B:THR39 2.1 94.0 1.0
PB B:GNP202 2.6 5.1 1.0
CG2 B:THR21 2.9 74.5 1.0
N3B B:GNP202 3.0 6.5 1.0
PG B:GNP202 3.0 6.4 1.0
N B:THR21 3.1 74.5 1.0
O1B B:GNP202 3.2 5.0 1.0
CB B:THR39 3.2 94.0 1.0
CB B:LYS20 3.4 79.3 1.0
CG2 B:THR39 3.7 94.0 1.0
CB B:THR21 3.8 74.5 1.0
N B:LYS20 3.9 79.3 1.0
CA B:LYS20 3.9 79.3 1.0
C B:LYS20 3.9 79.3 1.0
OG1 B:THR21 3.9 74.5 1.0
CA B:THR21 4.0 74.5 1.0
O2G B:GNP202 4.0 9.2 1.0
O3A B:GNP202 4.0 5.2 1.0
O1G B:GNP202 4.0 9.2 1.0
NZ B:LYS20 4.1 79.3 1.0
OD2 B:ASP63 4.5 100.0 1.0
CA B:THR39 4.5 94.0 1.0
CG B:LYS20 4.6 79.3 1.0
N B:THR39 4.6 94.0 1.0
O2A B:GNP202 4.7 6.4 1.0
PA B:GNP202 4.7 5.7 1.0
CD B:LYS20 4.8 79.3 1.0
O1A B:GNP202 4.8 6.9 1.0
C B:GLY19 4.9 86.3 1.0

Reference:

H.Zhu, F.Tonelli, M.Turk, A.Prescott, D.R.Alessi, J.Sun. RAB29-Dependent Asymmetrical Activation of Leucine-Rich Repeat Kinase 2. Science V. 382 1404 2023.
ISSN: ESSN 1095-9203
PubMed: 38127736
DOI: 10.1126/SCIENCE.ADI9926
Page generated: Fri Oct 4 02:49:02 2024

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