Research workbench
Structure of ATTPC1 with 1 mm CA2+
Analyse Structure of ATTPC1 with 1 mm CA2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FHK
- Type
- protein
- Length
- 1,350 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Two pore calcium channel protein 1,GFP; ATTPC1-cter
- UniProt
- Q94KI8
- Ligands
- CA
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 76% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Two pore calcium channel protein 1,GFP | protein | 663 | 76% helix, 1% strand | Q94KI8 |
| B, D | ATTPC1-cter | protein | 12 | 83% helix, 0% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, C
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 | 853 | 0.87 | 0.89 | 47 | empty |
| 2 | 1014 | 0.79 | 0.80 | 72 | empty |
| 3 | 598 | 0.79 | 0.84 | 44 | empty |
| 4 | 494 | 0.78 | 0.85 | 39 | empty |
| 5 | 671 | 0.73 | 0.79 | 60 | empty |
Interfaces
3 interfaces between chains.
- A–C · 4077 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 273 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 264 Ų buried · 0 hydrogen bonds · protein-protein
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 7FHK · PDBe 7FHK · UniProt Q94KI8
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