Fluorine in PDB 8d3x: Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State

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

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

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State (pdb code 8d3x). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State, PDB code: 8d3x:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State within 5.0Å range: probe atom residue distance (Å) B Occ A:F2101 b:37.1 occ:1.00 F1 A:MF42101 0.0 37.1 1.0 MG A:MF42101 1.8 37.1 1.0 OD1 A:ASP366 2.2 41.5 1.0 F3 A:MF42101 2.9 37.1 1.0 F4 A:MF42101 2.9 37.1 1.0 F2 A:MF42101 2.9 37.1 1.0 CG A:ASP366 3.0 41.5 1.0 OD2 A:ASP366 3.2 41.5 1.0 OG1 A:THR607 3.4 41.5 1.0 ND2 A:ASN710 3.6 43.6 1.0 CA A:THR607 3.6 41.5 1.0 N A:GLY608 3.9 46.0 1.0 CB A:THR607 3.9 41.5 1.0 NZ A:LYS688 4.0 41.5 1.0 C A:THR607 4.2 41.5 1.0 O A:THR209 4.2 49.6 1.0 O A:VAL606 4.4 41.5 1.0 CB A:ASP366 4.4 41.5 1.0 N A:LYS367 4.5 41.5 1.0 CG A:ASN710 4.5 43.6 1.0 OD1 A:ASN710 4.6 43.6 1.0 OG1 A:THR368 4.7 41.5 1.0 N A:THR607 4.7 41.5 1.0 CA A:ASP366 4.9 41.5 1.0 CE A:LYS688 4.9 41.5 1.0 CD A:LYS688 5.0 41.5 1.0 C A:VAL606 5.0 41.5 1.0

Fluorine binding site 2 out of 4 in the Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State within 5.0Å range: probe atom residue distance (Å) B Occ A:F2101 b:37.1 occ:1.00 F2 A:MF42101 0.0 37.1 1.0 MG A:MF42101 1.8 37.1 1.0 N A:THR368 2.3 41.5 1.0 OG1 A:THR368 2.5 41.5 1.0 OD2 A:ASP366 2.9 41.5 1.0 N A:LYS367 2.9 41.5 1.0 F3 A:MF42101 2.9 37.1 1.0 F4 A:MF42101 2.9 37.1 1.0 F1 A:MF42101 2.9 37.1 1.0 CG A:ASP366 3.0 41.5 1.0 OD1 A:ASP366 3.0 41.5 1.0 C A:LYS367 3.2 41.5 1.0 CA A:LYS367 3.2 41.5 1.0 CB A:LYS367 3.2 41.5 1.0 CA A:THR368 3.3 41.5 1.0 CB A:THR368 3.3 41.5 1.0 O A:THR368 3.6 41.5 1.0 OG1 A:THR607 3.7 41.5 1.0 C A:ASP366 3.9 41.5 1.0 C A:THR368 3.9 41.5 1.0 CB A:ASP366 4.0 41.5 1.0 CG2 A:THR368 4.0 41.5 1.0 CG A:LYS367 4.1 41.5 1.0 O A:GLY210 4.3 48.4 1.0 O A:LYS367 4.3 41.5 1.0 CA A:ASP366 4.3 41.5 1.0 CB A:THR607 4.5 41.5 1.0 O A:ASP366 4.8 41.5 1.0

Fluorine binding site 3 out of 4 in the Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State within 5.0Å range: probe atom residue distance (Å) B Occ A:F2101 b:37.1 occ:1.00 F3 A:MF42101 0.0 37.1 1.0 MG A:MF42101 1.8 37.1 1.0 O A:GLY210 2.4 48.4 1.0 O A:THR209 2.8 49.6 1.0 F1 A:MF42101 2.9 37.1 1.0 F2 A:MF42101 2.9 37.1 1.0 F4 A:MF42101 2.9 37.1 1.0 C A:GLY210 3.0 48.4 1.0 OG1 A:THR368 3.0 41.5 1.0 CA A:GLY210 3.1 48.4 1.0 C A:THR209 3.7 49.6 1.0 OG1 A:THR607 3.8 41.5 1.0 N A:GLY210 3.9 48.4 1.0 CD A:GLU211 3.9 51.8 1.0 OE2 A:GLU211 4.1 51.8 1.0 CG A:GLU211 4.1 51.8 1.0 N A:GLU211 4.1 51.8 1.0 OE1 A:GLU211 4.2 51.8 1.0 CB A:THR368 4.3 41.5 1.0 ND2 A:ASN710 4.3 43.6 1.0 CG2 A:THR368 4.4 41.5 1.0 OD2 A:ASP366 4.6 41.5 1.0 N A:GLY608 4.6 46.0 1.0 OD1 A:ASP366 4.6 41.5 1.0 N A:THR368 4.7 41.5 1.0 CA A:GLU211 4.8 51.8 1.0 CG A:ASP366 5.0 41.5 1.0

Fluorine binding site 4 out of 4 in the Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Human ALPHA3 Na+/K+-Atpase in Its K+-Occluded State within 5.0Å range: probe atom residue distance (Å) B Occ A:F2101 b:37.1 occ:1.00 F4 A:MF42101 0.0 37.1 1.0 MG A:MF42101 1.8 37.1 1.0 OD2 A:ASP366 2.3 41.5 1.0 F2 A:MF42101 2.9 37.1 1.0 F1 A:MF42101 2.9 37.1 1.0 F3 A:MF42101 2.9 37.1 1.0 OG1 A:THR368 3.1 41.5 1.0 CG A:ASP366 3.3 41.5 1.0 OD1 A:ASP707 3.5 41.5 1.0 OD1 A:ASP366 3.6 41.5 1.0 O A:GLY210 3.7 48.4 1.0 ND2 A:ASN710 3.8 43.6 1.0 CA A:GLY210 4.1 48.4 1.0 O A:THR368 4.1 41.5 1.0 OD1 A:ASN710 4.2 43.6 1.0 C A:GLY210 4.3 48.4 1.0 N A:GLY708 4.4 42.9 1.0 CG A:ASN710 4.4 43.6 1.0 CB A:THR368 4.5 41.5 1.0 CA A:GLY708 4.6 42.9 1.0 N A:THR368 4.7 41.5 1.0 CB A:ASP366 4.7 41.5 1.0 CG A:ASP707 4.7 41.5 1.0 O A:THR209 4.9 49.6 1.0 CA A:THR368 5.0 41.5 1.0 C A:THR368 5.0 41.5 1.0

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