Research workbench
Structure of ATTPC1 D240A/D454A/E528A mutant with 1 mm CA2+
Analyse Structure of ATTPC1 D240A/D454A/E528A mutant 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
- 7FHN
- Type
- protein
- Length
- 1,294 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Two pore calcium channel protein 1,GFP
- UniProt
- Q94KI8
- Ligands
- CA
- Pockets
- 19 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 72% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Two pore calcium channel protein 1,GFP | protein | 647 | 72% helix, 1% strand | Q94KI8 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1151 | 0.85 | 0.86 | 70 | empty |
| 2 | 272 | 0.76 | 0.88 | 35 | empty |
| 3 | 1103 | 0.76 | 0.78 | 87 | empty |
| 4 | 252 | 0.74 | 0.88 | 33 | empty |
| 5 | 786 | 0.72 | 0.77 | 64 | empty |
Interfaces
1 interface between chains.
- A–C · 3804 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7FHN · Structure of AtTPC1 D240A/D454A/E528A mutant with 1 mM Ca2+ · the same entry in another collection · chain A against A, TM-score 1.00
- Q94KI8 · AlphaFold monomer V2.0 prediction for two pore calcium channel protein 1 (Q94KI8) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 7FHN · PDBe 7FHN · UniProt Q94KI8
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