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Magnesium in PDB 8vh4: Cryo-Em Structure of RAB12-LRRK2 Complex in the LRRK2 Monomer State

Enzymatic activity of Cryo-Em Structure of RAB12-LRRK2 Complex in the LRRK2 Monomer State

All present enzymatic activity of Cryo-Em Structure of RAB12-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 RAB12-LRRK2 Complex in the LRRK2 Monomer State (pdb code 8vh4). 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 RAB12-LRRK2 Complex in the LRRK2 Monomer State, PDB code: 8vh4:

Magnesium binding site 1 out of 1 in 8vh4

Go back to Magnesium Binding Sites List in 8vh4
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of RAB12-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 RAB12-LRRK2 Complex in the LRRK2 Monomer State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:93.3
occ:1.00
O2B B:GNP302 2.0 96.2 1.0
O1A B:GNP302 2.1 96.2 1.0
O2G B:GNP302 2.1 96.2 1.0
N3B B:GNP302 2.1 96.2 1.0
PB B:GNP302 2.4 96.2 1.0
PG B:GNP302 2.4 96.2 1.0
OG1 B:THR56 2.7 89.4 1.0
PA B:GNP302 3.1 96.2 1.0
O3G B:GNP302 3.1 96.2 1.0
O3A B:GNP302 3.2 96.2 1.0
CB B:THR56 3.4 89.4 1.0
O2A B:GNP302 3.7 96.2 1.0
O1B B:GNP302 3.8 96.2 1.0
O1G B:GNP302 3.8 96.2 1.0
N B:THR56 3.8 89.4 1.0
CA B:THR56 4.3 89.4 1.0
SG B:CYS71 4.3 101.7 1.0
O5' B:GNP302 4.4 96.2 1.0
CA B:SER73 4.5 92.4 1.0
N B:THR74 4.5 86.3 1.0
CG2 B:THR56 4.6 89.4 1.0
CG2 B:THR74 4.6 86.3 1.0
N B:LYS55 4.6 85.1 1.0
OG B:SER73 4.8 92.4 1.0
OG1 B:THR74 4.8 86.3 1.0
C B:LYS55 5.0 85.1 1.0
O B:LYS72 5.0 97.6 1.0

Reference:

X.Li, H.Zhu, B.T.Huang, X.Li, H.Kim, H.Tan, Y.Zhang, I.Choi, J.Peng, P.Xu, J.Sun, Z.Yue. RAB12-LRRK2 Complex Suppresses Primary Ciliogenesis and Regulates Centrosome Homeostasis in Astrocytes. Nat Commun V. 15 8434 2024.
ISSN: ESSN 2041-1723
PubMed: 39343966
DOI: 10.1038/S41467-024-52723-6
Page generated: Fri Aug 15 17:37:37 2025

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