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Aluminium in PDB 8ies: Cryo-Em Structure of ATP13A2 in the E1P-Adp State

Other elements in 8ies:

The structure of Cryo-Em Structure of ATP13A2 in the E1P-Adp State also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Fluorine (F) 4 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Cryo-Em Structure of ATP13A2 in the E1P-Adp State (pdb code 8ies). 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 ATP13A2 in the E1P-Adp State, PDB code: 8ies:

Aluminium binding site 1 out of 1 in 8ies

Go back to Aluminium Binding Sites List in 8ies
Aluminium binding site 1 out of 1 in the Cryo-Em Structure of ATP13A2 in the E1P-Adp 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 ATP13A2 in the E1P-Adp State within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Al1201

b:56.6
occ:1.00
AL P:ALF1201 0.0 56.6 1.0
F3 P:ALF1201 1.8 56.6 1.0
F2 P:ALF1201 1.8 56.6 1.0
F4 P:ALF1201 1.8 56.6 1.0
F1 P:ALF1201 1.8 56.6 1.0
O1B P:ADP1203 2.6 62.8 1.0
OD2 P:ASP513 2.7 51.6 1.0
OD1 P:ASP513 2.7 51.6 1.0
O2B P:ADP1203 2.9 62.8 1.0
CG P:ASP513 2.9 51.6 1.0
PB P:ADP1203 3.0 62.8 1.0
MG P:MG1202 3.3 63.1 1.0
O3B P:ADP1203 3.6 62.8 1.0
O P:THR515 3.8 52.5 1.0
N P:THR515 3.9 52.5 1.0
CB P:ASP513 4.1 51.6 1.0
N P:LYS514 4.2 52.0 1.0
CB P:THR515 4.4 52.5 1.0
O3A P:ADP1203 4.5 62.8 1.0
CA P:THR515 4.6 52.5 1.0
ND2 P:ASN881 4.6 60.0 1.0
OD1 P:ASN881 4.6 60.0 1.0
OG1 P:THR750 4.6 47.2 1.0
C P:THR515 4.6 52.5 1.0
O1A P:ADP1203 4.9 62.8 1.0
C P:LYS514 4.9 52.0 1.0
CA P:LYS514 4.9 52.0 1.0
CA P:ASP513 4.9 51.6 1.0
CB P:LYS514 5.0 52.0 1.0
OG1 P:THR515 5.0 52.5 1.0

Reference:

J.Mu, C.Xue, L.Fu, Z.Yu, M.Nie, M.Wu, X.Chen, K.Liu, R.Bu, Y.Huang, B.Yang, J.Han, Q.Jiang, K.C.Chan, R.Zhou, H.Li, A.Huang, Y.Wang, Z.Liu. Conformational Cycle of Human Polyamine Transporter ATP13A2. Nat Commun V. 14 1978 2023.
ISSN: ESSN 2041-1723
PubMed: 37031211
DOI: 10.1038/S41467-023-37741-0
Page generated: Sun Jul 6 22:21:45 2025

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