Research workbench
Structure of ATTPC1(DDE) in state 2
Analyse Structure of ATTPC1(DDE) in state 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E1P
- Type
- protein
- Length
- 1,292 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Two pore calcium channel protein 1
- UniProt
- Q94KI8
- Ligands
- PLM, CA
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Two pore calcium channel protein 1 | protein | 646 | 68% helix, 0% strand | Q94KI8 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 16 copies · chains A, B
- CA · Calcium ion · metal · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 624 | 0.88 | 0.93 | 40 | empty |
| 2 | 1056 | 0.81 | 0.81 | 88 | PLM |
| 3 | 992 | 0.79 | 0.80 | 87 | PLM |
| 4 | 190 | 0.77 | 0.92 | 33 | empty |
| 5 | 167 | 0.76 | 0.92 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 4029 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 4 lipid (phosphorylation, palmitoylation).
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 Q94KI8
- Elsewhere: RCSB PDB 6E1P · PDBe 6E1P · UniProt Q94KI8
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