Research workbench
Cryo-EM structure of the human ATP13A2 (E1-ATP state)
Analyse Cryo-EM structure of the human ATP13A2 (E1-ATP state) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VPI
- Type
- protein
- Length
- 959 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyamine-transporting ATPase 13A2
- EC
- 7.6.2.-
- UniProt
- Q9NQ11
- Ligands
- ACP, MG
- Pockets
- 11 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyamine-transporting ATPase 13A2 (EC 7.6.2.-) | protein | 959 | 48% helix, 16% strand | Q9NQ11 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · 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
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1141 | 0.83 | 0.84 | 119 | ACP, MG |
| 2 | 642 | 0.69 | 0.77 | 73 | empty |
| 3 | 278 | 0.65 | 0.82 | 39 | empty |
| 4 | 570 | 0.64 | 0.76 | 52 | empty |
| 5 | 225 | 0.58 | 0.79 | 23 | empty |
Compared structures
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 7VPI · PDBe 7VPI · UniProt Q9NQ11
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