Research workbench
ATTPC1 D454N with 1 mm CA2+
Analyse ATTPC1 D454N 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
- 7TBG
- Type
- protein
- Length
- 1,190 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Two pore calcium channel protein 1
- UniProt
- Q94KI8
- Ligands
- CA, NA
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Two pore calcium channel protein 1 | protein | 595 | 75% helix, 0% strand | Q94KI8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 852 | 0.87 | 0.89 | 43 | empty |
| 2 | 606 | 0.75 | 0.81 | 47 | empty |
| 3 | 572 | 0.74 | 0.80 | 41 | empty |
| 4 | 374 | 0.69 | 0.80 | 36 | empty |
| 5 | 353 | 0.67 | 0.80 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 3832 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 7TBG · PDBe 7TBG · UniProt Q94KI8
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