Magnesium in PDB 7to2: Cryo-Em Structure of Rig-I Bound to the Internal Sites of P3SLR30 (+Atp)

Enzymatic activity of Cryo-Em Structure of Rig-I Bound to the Internal Sites of P3SLR30 (+Atp)

All present enzymatic activity of Cryo-Em Structure of Rig-I Bound to the Internal Sites of P3SLR30 (+Atp):
3.6.4.13;

Other elements in 7to2:

The structure of Cryo-Em Structure of Rig-I Bound to the Internal Sites of P3SLR30 (+Atp) also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Rig-I Bound to the Internal Sites of P3SLR30 (+Atp) (pdb code 7to2). 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 Rig-I Bound to the Internal Sites of P3SLR30 (+Atp), PDB code: 7to2:

Magnesium binding site 1 out of 1 in 7to2

Go back to Magnesium Binding Sites List in 7to2
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of Rig-I Bound to the Internal Sites of P3SLR30 (+Atp)


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 Rig-I Bound to the Internal Sites of P3SLR30 (+Atp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:46.2
occ:1.00
O2B A:ADP1003 2.9 71.4 1.0
OE1 A:GLU373 3.3 46.2 1.0
OD2 A:ASP372 3.5 42.2 1.0
PB A:ADP1003 4.0 73.2 1.0
O3A A:ADP1003 4.1 75.2 1.0
OD1 A:ASP372 4.1 42.2 1.0
CG A:ASP372 4.2 41.2 1.0
O1A A:ADP1003 4.3 77.1 1.0
CD A:GLU373 4.3 46.4 1.0
O2A A:ADP1003 4.5 74.0 1.0
PA A:ADP1003 4.5 76.0 1.0
O3B A:ADP1003 4.5 75.2 1.0
OG1 A:THR271 4.6 49.9 1.0
CG A:GLU373 4.8 44.3 1.0
NZ A:LYS270 4.9 45.3 1.0
CE A:LYS270 4.9 44.8 1.0

Reference:

W.Wang, A.M.Pyle. The Rig-I Receptor Adopts Two Different Conformations For Distinguishing Host From Viral Rna Ligands. Mol.Cell V. 82 4131 2022.
ISSN: ISSN 1097-2765
PubMed: 36272408
DOI: 10.1016/J.MOLCEL.2022.09.029
Page generated: Thu Apr 6 23:03:18 2023

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