Research workbench
Structure of rabbit ryanodine receptor RYR1 open state activated by calcium ion
Analyse Structure of rabbit ryanodine receptor RYR1 open state activated by calcium ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5J8V
- Type
- protein
- Length
- 13,812 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ryanodine receptor 1
- UniProt
- P11716
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 55% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Ryanodine receptor 1 | protein | 3453 | 55% helix, 4% strand | P11716 |
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 | 815 | 0.84 | 0.86 | 120 | empty |
| 2 | 1002 | 0.84 | 0.85 | 113 | empty |
| 3 | 952 | 0.84 | 0.85 | 110 | empty |
| 4 | 695 | 0.83 | 0.86 | 103 | empty |
| 5 | 1008 | 0.82 | 0.83 | 135 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1423 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 1420 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 1408 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 1406 Ų buried · 5 hydrogen bonds · protein-protein
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 P11716
- Elsewhere: RCSB PDB 5J8V · PDBe 5J8V · UniProt P11716
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