Research workbench
Reovirus core
Analyse Reovirus core in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EJ6
- Type
- protein
- Length
- 4,370 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LAMBDA2; LAMBDA1; SIGMA2
- UniProt
- P11079, P15024, P03525
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LAMBDA2 | protein | 1284 | 25% helix, 26% strand | P11079 |
| B | LAMBDA1 | protein | 1031 | 38% helix, 16% strand | P15024 |
| C | LAMBDA1 | protein | 1221 | 35% helix, 16% strand | P15024 |
| D, E | SIGMA2 | protein | 417 | 47% helix, 13% strand | P03525 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains C
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 | 295 | 0.85 | 0.95 | 44 | empty |
| 2 | 1022 | 0.84 | 0.85 | 116 | empty |
| 3 | 754 | 0.83 | 0.86 | 59 | empty |
| 4 | 580 | 0.82 | 0.88 | 49 | empty |
| 5 | 179 | 0.81 | 0.96 | 32 | empty |
Interfaces
6 interfaces between chains.
- B–C · 3446 Ų buried · 38 hydrogen bonds · protein-protein
- B–D · 3217 Ų buried · 34 hydrogen bonds · protein-protein
- C–E · 1416 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1372 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 712 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1EJ6 · Reovirus core · 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 P11079
- Every structure of UniProt P15024
- Every structure of UniProt P03525
- Elsewhere: RCSB PDB 1EJ6 · PDBe 1EJ6 · UniProt P11079 · UniProt P15024 · UniProt P03525
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.