Aluminium in PDB 7x22: Cryo-Em Structure of Non Gastric H,K-Atpase ALPHA2 K794S in (2K+)E2- Alf State

All present enzymatic activity of Cryo-Em Structure of Non Gastric H,K-Atpase ALPHA2 K794S in (2K+)E2- Alf State:
7.2.2.13; 7.2.2.19;

The structure of Cryo-Em Structure of Non Gastric H,K-Atpase ALPHA2 K794S in (2K+)E2- Alf State also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Fluorine	(F)	4 atoms
Potassium	(K)	3 atoms

The binding sites of Aluminium atom in the Cryo-Em Structure of Non Gastric H,K-Atpase ALPHA2 K794S in (2K+)E2- Alf State (pdb code 7x22). 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 Cryo-Em Structure of Non Gastric H,K-Atpase ALPHA2 K794S in (2K+)E2- Alf State, PDB code: 7x22:

Aluminium binding site 1 out of 1 in the Cryo-Em Structure of Non Gastric H,K-Atpase ALPHA2 K794S in (2K+)E2- Alf State


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Cryo-Em Structure of Non Gastric H,K-Atpase ALPHA2 K794S in (2K+)E2- Alf State within 5.0Å range: probe atom residue distance (Å) B Occ A:Al1101 b:84.5 occ:1.00 AL A:ALF1101 0.0 84.5 1.0 F3 A:ALF1101 1.8 84.5 1.0 F1 A:ALF1101 1.8 84.5 1.0 F2 A:ALF1101 1.8 84.5 1.0 F4 A:ALF1101 1.8 84.5 1.0 OD1 A:ASP388 2.4 77.8 1.0 OD2 A:ASP388 2.4 77.8 1.0 CG A:ASP388 2.7 77.8 1.0 MG A:MG1102 2.8 85.8 1.0 O A:THR390 3.8 81.1 1.0 ND2 A:ASN732 4.1 84.7 1.0 O A:GLY232 4.1 88.9 1.0 CA A:GLY232 4.1 88.9 1.0 O A:THR231 4.1 87.5 1.0 CB A:ASP388 4.1 77.8 1.0 N A:THR390 4.2 81.1 1.0 CB A:THR390 4.3 81.1 1.0 C A:GLY232 4.4 88.9 1.0 CA A:THR390 4.6 81.1 1.0 C A:THR390 4.7 81.1 1.0 N A:LYS389 4.7 78.6 1.0 OD1 A:ASN732 4.7 84.7 1.0 OD2 A:ASP733 4.7 85.0 1.0 N A:GLY630 4.8 85.5 1.0 OG1 A:THR629 4.8 81.2 1.0 OE2 A:GLU233 4.8 93.5 1.0 OD1 A:ASP733 4.8 85.0 1.0 CG A:ASN732 4.8 84.7 1.0 C A:THR231 5.0 87.5 1.0

V.C.Young, H.Nakanishi, D.J.Meyer, T.Nishizawa, A.Oshima, P.Artigas, K.Abe. Structure and Function of H + /K + Pump Mutants Reveal Na + /K + Pump Mechanisms. Nat Commun V. 13 5270 2022.
ISSN: ESSN 2041-1723
PubMed: 36085139
DOI: 10.1038/S41467-022-32793-0