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Aluminium in PDB 8d3u: Human ALPHA3 Na+/K+-Atpase in Its Na+-Occluded State

Enzymatic activity of Human ALPHA3 Na+/K+-Atpase in Its Na+-Occluded State

All present enzymatic activity of Human ALPHA3 Na+/K+-Atpase in Its Na+-Occluded State:
7.2.2.13;

Other elements in 8d3u:

The structure of Human ALPHA3 Na+/K+-Atpase in Its Na+-Occluded State also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Human ALPHA3 Na+/K+-Atpase in Its Na+-Occluded State (pdb code 8d3u). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Human ALPHA3 Na+/K+-Atpase in Its Na+-Occluded State, PDB code: 8d3u:

Aluminium binding site 1 out of 1 in 8d3u

Go back to Aluminium Binding Sites List in 8d3u
Aluminium binding site 1 out of 1 in the Human ALPHA3 Na+/K+-Atpase in Its Na+-Occluded State


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Human ALPHA3 Na+/K+-Atpase in Its Na+-Occluded State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1102

b:56.8
occ:1.00
AL A:ALF1102 0.0 56.8 1.0
F1 A:ALF1102 1.8 56.8 1.0
F4 A:ALF1102 1.8 56.8 1.0
F3 A:ALF1102 1.8 56.8 1.0
F2 A:ALF1102 1.8 56.8 1.0
O2B A:ADP1101 2.5 57.2 1.0
OD2 A:ASP366 2.5 56.8 1.0
OD1 A:ASP366 2.7 56.8 1.0
CG A:ASP366 2.8 56.8 1.0
O A:THR368 3.5 56.8 1.0
PB A:ADP1101 3.6 57.2 1.0
ND2 A:ASN710 3.6 56.8 1.0
OD1 A:ASP707 3.9 57.3 1.0
O1B A:ADP1101 3.9 57.2 1.0
O3A A:ADP1101 3.9 57.2 1.0
CB A:ASP366 4.1 56.8 1.0
CG2 A:THR368 4.2 56.8 1.0
OD1 A:ASN710 4.3 56.8 1.0
CG A:ASN710 4.4 56.8 1.0
C A:THR368 4.6 56.8 1.0
N A:THR368 4.7 56.8 1.0
NZ A:LYS688 4.7 56.8 1.0
N A:LYS367 4.9 56.8 1.0
O3B A:ADP1101 4.9 57.2 1.0

Reference:

P.T.Nguyen, C.Deisl, M.Fine, T.S.Tippetts, E.Uchikawa, X.C.Bai, B.Levine. Structural Basis For Gating Mechanism of the Human Sodium-Potassium Pump. Nat Commun V. 13 5293 2022.
ISSN: ESSN 2041-1723
PubMed: 36075933
DOI: 10.1038/S41467-022-32990-X
Page generated: Tue Apr 4 16:36:39 2023

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