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Magnesium in PDB 7usd: Cryo-Em Structure of D-Site RAC1-Bound Wave Regulatory Complex

Enzymatic activity of Cryo-Em Structure of D-Site RAC1-Bound Wave Regulatory Complex

All present enzymatic activity of Cryo-Em Structure of D-Site RAC1-Bound Wave Regulatory Complex:
3.6.5.2;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of D-Site RAC1-Bound Wave Regulatory Complex (pdb code 7usd). 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 D-Site RAC1-Bound Wave Regulatory Complex, PDB code: 7usd:

Magnesium binding site 1 out of 1 in 7usd

Go back to Magnesium Binding Sites List in 7usd
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of D-Site RAC1-Bound Wave Regulatory Complex


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 D-Site RAC1-Bound Wave Regulatory Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg202

b:100.9
occ:1.00
O1G F:GTP201 2.3 101.9 1.0
OG1 F:THR35 2.4 96.0 1.0
O2G F:GTP201 2.5 101.9 1.0
O2B F:GTP201 2.6 101.9 1.0
OG1 F:THR17 2.7 100.8 1.0
PG F:GTP201 2.8 101.9 1.0
O3B F:GTP201 3.4 101.9 1.0
PB F:GTP201 3.4 101.9 1.0
OD1 F:ASP57 3.4 98.3 1.0
CB F:THR35 3.5 96.0 1.0
CG2 F:THR35 3.7 96.0 1.0
OD2 F:ASP57 3.8 98.3 1.0
CG F:ASP57 3.9 98.3 1.0
O1B F:GTP201 4.0 101.9 1.0
N F:THR35 4.0 96.0 1.0
O F:THR58 4.0 97.7 1.0
CB F:THR17 4.1 100.8 1.0
NZ F:LYS16 4.1 99.3 1.0
O3G F:GTP201 4.2 101.9 1.0
CA F:THR35 4.3 96.0 1.0
O F:THR35 4.4 96.0 1.0
CE F:LYS16 4.5 99.3 1.0
N F:THR17 4.6 100.8 1.0
C F:THR35 4.7 96.0 1.0
C F:THR58 4.8 97.7 1.0
O3A F:GTP201 4.8 101.9 1.0
CA F:THR17 4.9 100.8 1.0
CA F:ALA59 4.9 98.4 1.0

Reference:

B.Ding, S.Yang, M.Schaks, Y.Liu, A.J.Brown, K.Rottner, S.Chowdhury, B.Chen. Structures Reveal A Key Mechanism of Wave Regulatory Complex Activation By RAC1 Gtpase. Nat Commun V. 13 5444 2022.
ISSN: ESSN 2041-1723
PubMed: 36114192
DOI: 10.1038/S41467-022-33174-3
Page generated: Thu Oct 3 10:12:32 2024

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