Research workbench
Cryo-EM structure of ATP13A2 D508N mutant in the E1-ATP-like state
Analyse Cryo-EM structure of ATP13A2 D508N mutant in the E1-ATP-like state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N74
- Type
- protein
- Length
- 1,036 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 3 of polyamine-transporting ATPase 13A2
- EC
- 7.6.2.-
- UniProt
- Q9NQ11
- Ligands
- Y01, ATP, MG
- Pockets
- 16 · best druggability 0.81
Structure
electron microscopy · 1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 3 of polyamine-transporting ATPase 13A2 (EC 7.6.2.-) | protein | 1036 | 47% helix, 19% strand | Q9NQ11 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 2 copies · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1140 | 0.81 | 0.82 | 93 | ATP, MG |
| 2 | 249 | 0.62 | 0.81 | 26 | empty |
| 3 | 361 | 0.61 | 0.77 | 45 | empty |
| 4 | 189 | 0.60 | 0.82 | 28 | empty |
| 5 | 274 | 0.55 | 0.76 | 40 | empty |
Compared structures
- 7N74 · Cryo-EM structure of ATP13A2 D508N mutant in the E1-ATP-like 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 0.94
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 7N74 · PDBe 7N74 · UniProt Q9NQ11
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