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Magnesium in PDB 8ox4: Cryo-Em Structure of ATP8B1-CDC50A in E1-Atp Conformation

Enzymatic activity of Cryo-Em Structure of ATP8B1-CDC50A in E1-Atp Conformation

All present enzymatic activity of Cryo-Em Structure of ATP8B1-CDC50A in E1-Atp Conformation:
7.6.2.1;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of ATP8B1-CDC50A in E1-Atp Conformation (pdb code 8ox4). 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 ATP8B1-CDC50A in E1-Atp Conformation, PDB code: 8ox4:

Magnesium binding site 1 out of 1 in 8ox4

Go back to Magnesium Binding Sites List in 8ox4
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of ATP8B1-CDC50A in E1-Atp Conformation


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 ATP8B1-CDC50A in E1-Atp Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1202

b:24.2
occ:1.00
OD2 A:ASP454 1.9 34.9 1.0
O A:THR456 2.4 46.0 1.0
O3G A:ACP1201 2.5 71.9 1.0
OE1 A:GLU914 2.9 53.7 1.0
OD1 A:ASP893 3.0 35.6 1.0
CG A:ASP454 3.1 34.9 1.0
O A:ASP893 3.3 35.6 1.0
C3B A:ACP1201 3.3 71.9 1.0
PG A:ACP1201 3.5 71.9 1.0
C A:THR456 3.5 46.0 1.0
OE2 A:GLU914 3.5 53.7 1.0
CD A:GLU914 3.6 53.7 1.0
OD2 A:ASP897 3.8 37.3 1.0
OD1 A:ASP454 3.9 34.9 1.0
CG A:ASP893 4.1 35.6 1.0
CB A:ASP454 4.2 34.9 1.0
ND2 A:ASN896 4.2 46.0 1.0
OD1 A:ASN896 4.3 46.0 1.0
C A:ASP893 4.3 35.6 1.0
CA A:THR456 4.3 46.0 1.0
CB A:THR456 4.4 46.0 1.0
O2G A:ACP1201 4.5 71.9 1.0
N A:THR456 4.5 46.0 1.0
N A:GLY457 4.5 35.7 1.0
O1G A:ACP1201 4.6 71.9 1.0
OD2 A:ASP893 4.6 35.6 1.0
CA A:GLY457 4.7 35.7 1.0
CG A:ASN896 4.7 46.0 1.0
CG A:ASP897 4.8 37.3 1.0
N A:ASP893 4.9 35.6 1.0

Reference:

T.Dieudonne, F.Kummerer, M.J.Laursen, C.Stock, R.K.Flygaard, S.Khalid, G.Lenoir, J.A.Lyons, K.Lindorff-Larsen, P.Nissen. Activation and Substrate Specificity of the Human P4-Atpase ATP8B1. Nat Commun V. 14 7492 2023.
ISSN: ESSN 2041-1723
PubMed: 37980352
DOI: 10.1038/S41467-023-42828-9
Page generated: Fri Oct 4 15:09:17 2024

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