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Aluminium in PDB 7x20: Crystal Structure of Non Gastric H,K-Atpase ALPHA2 in (K+)E2-Alf State

Enzymatic activity of Crystal Structure of Non Gastric H,K-Atpase ALPHA2 in (K+)E2-Alf State

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

Protein crystallography data

The structure of Crystal Structure of Non Gastric H,K-Atpase ALPHA2 in (K+)E2-Alf State, PDB code: 7x20 was solved by H.Nakanishi, K.Abe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.06 / 3.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 75.97, 109.06, 267.67, 90, 90, 90
R / Rfree (%) 26.5 / 31.6

Other elements in 7x20:

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

Fluorine (F) 4 atoms
Potassium (K) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Crystal Structure of Non Gastric H,K-Atpase ALPHA2 in (K+)E2-Alf State (pdb code 7x20). 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 Crystal Structure of Non Gastric H,K-Atpase ALPHA2 in (K+)E2-Alf State, PDB code: 7x20:

Aluminium binding site 1 out of 1 in 7x20

Go back to Aluminium Binding Sites List in 7x20
Aluminium binding site 1 out of 1 in the Crystal Structure of Non Gastric H,K-Atpase ALPHA2 in (K+)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 Crystal Structure of Non Gastric H,K-Atpase ALPHA2 in (K+)E2-Alf State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1101

b:25.1
occ:1.00
 AL A:ALF1101 0.0 25.1 1.0
F4 A:ALF1101 1.8 26.6 1.0
F3 A:ALF1101 1.8 24.9 1.0
F1 A:ALF1101 1.8 21.5 1.0
F2 A:ALF1101 1.8 19.2 1.0
OD1 A:ASP388 2.2 24.1 1.0
OD2 A:ASP388 2.5 23.9 1.0
CG A:ASP388 2.7 23.8 1.0
OG1 A:THR390 2.8 28.5 1.0
OG1 A:THR629 3.5 24.0 1.0
O A:THR231 3.8 27.4 1.0
O A:THR390 3.8 25.3 1.0
OD1 A:ASP729 3.8 26.0 1.0
N A:THR390 4.0 26.3 1.0
ND2 A:ASN732 4.1 23.0 1.0
CA A:GLY232 4.1 31.9 1.0
CB A:ASP388 4.2 23.5 1.0
CB A:THR390 4.2 26.8 1.0
OE2 A:GLU233 4.3 34.7 1.0
OD2 A:ASP733 4.4 23.1 1.0
N A:LYS389 4.4 25.3 1.0
O A:GLY232 4.5 35.6 1.0
CA A:THR390 4.5 26.6 1.0
CB A:THR629 4.5 24.2 1.0
C A:THR390 4.6 26.0 1.0
C A:GLY232 4.6 33.3 1.0
OD1 A:ASN732 4.7 24.9 1.0
C A:THR231 4.7 28.5 1.0
CG A:ASN732 4.8 22.9 1.0
N A:GLY232 4.9 28.8 1.0
CA A:ASP388 4.9 23.9 1.0
C A:LYS389 4.9 26.4 1.0
CG A:ASP729 4.9 27.0 1.0
N A:GLY630 5.0 23.7 1.0

Reference:

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
Page generated: Wed Jul 10 10:12:55 2024

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