Research workbench
Structure of full-length IP3R1 channel in the apo-state determined by single particle cryo-EM
Analyse Structure of full-length IP3R1 channel in the apo-state determined by single… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JAV
- Type
- protein
- Length
- 9,308 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol 1,4,5-trisphosphate receptor type 1
- UniProt
- P29994
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 15% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Inositol 1,4,5-trisphosphate receptor type 1 | protein | 2327 | 15% helix, 1% strand | P29994 |
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 | 942 | 0.88 | 0.89 | 144 | empty |
| 2 | 459 | 0.84 | 0.91 | 52 | empty |
| 3 | 163 | 0.82 | 0.97 | 64 | empty |
| 4 | 158 | 0.81 | 0.97 | 62 | empty |
| 5 | 161 | 0.81 | 0.97 | 63 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3934 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 3932 Ų buried · 25 hydrogen bonds · protein-protein
- A–D · 3931 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 3911 Ų buried · 27 hydrogen bonds · protein-protein
- B–D · 603 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3JAV · Structure of full-length IP3R1 channel in the apo-state determined by single particle… · the same entry in another collection · chain A against A, TM-score 1.00
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 P29994
- Elsewhere: RCSB PDB 3JAV · PDBe 3JAV · UniProt P29994
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