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Cryo-EM structure of ATP13A2 in the E2-pi state

Analyse Cryo-EM structure of ATP13A2 in the E2-pi state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7N78
Type: protein
Length: 1,030 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9NQ11
Ligands: Y01, PC1, SPM, MG, PO4

Structure

electron microscopy · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	1030	—	Q9NQ11

Ligands and binding sites

Y01 · Cholesterol hemisuccinate · ligand · 3 copies · chains A
PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 2 copies · chains A
SPM · Spermine · ligand · chains A
MG · Magnesium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A
LMT · Dodecyl-beta-D-maltoside · additive · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7N78 · Cryo-EM structure of ATP13A2 in the E2-Pi state · the same entry in another collection · chain A against A, TM-score 1.00
Q9NQ11 · AlphaFold monomer V2.0 prediction for polyamine-transporting ATPase 13A2 (Q9NQ11) · a predicted model of the same protein · chain A against A, TM-score 0.83

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9NQ11
Elsewhere: RCSB PDB 7N78 · PDBe 7N78 · UniProt Q9NQ11

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