Research workbench
IP3, ATP, and Ca2+ bound type 3 IP3 receptor in the active state
Analyse IP3, ATP, and Ca2+ bound type 3 IP3 receptor in the active state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7T3T
- Type
- protein
- Length
- 8,484 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.8
- Source
- Homo sapiens
- Molecule
- Inositol 1,4,5-trisphosphate receptor type 3
- UniProt
- Q14573
- Ligands
- I3P, ATP, ZN, CA
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · resolution 3.8 · 1 distinct chain · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Inositol 1,4,5-trisphosphate receptor type 3 | protein | 2121 | 59% helix, 9% strand | Q14573 |
Ligands and binding sites
- I3P · D-myo-inositol-1,4,5-triphosphate · ligand · 4 copies · chains A, B, C, D
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1020 | 0.79 | 0.81 | 56 | empty |
| 2 | 530 | 0.75 | 0.83 | 47 | empty |
| 3 | 531 | 0.74 | 0.82 | 45 | empty |
| 4 | 1008 | 0.72 | 0.76 | 91 | empty |
| 5 | 1160 | 0.72 | 0.76 | 104 | empty |
Interfaces
4 interfaces between chains.
- A–D · 3380 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 3374 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 3369 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 3365 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- Q14573 · AlphaFold monomer V2.0 prediction for inositol 1,4,5-trisphosphate receptor type 3… · a predicted model of the same protein · chain A against A, TM-score 0.80
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 Q14573
- Elsewhere: RCSB PDB 7T3T · PDBe 7T3T · UniProt Q14573
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