MolNFT v1 · #16048 · protein
Cryoem structure of poliovirus receptor bound to poliovirus
1NN8: “Cryoem structure of poliovirus receptor bound to poliovirus”. Electron microscopy, 1 ligand (MYR), 5 pockets (best druggability 0.80). MolNFT v1 #16048 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NN8
- Type
- protein
- Length
- 1,756 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Poliovirus receptor; Coat protein VP1; Coat protein VP2; Coat protein VP3; Coat protein…
- UniProt
- P15151, P03300
- Ligands
- MYR
- Pockets
- 5 · best druggability 0.80
Structure
electron microscopy · 5 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R, S, T | Poliovirus receptor | protein | 301 | 0% helix, 0% strand | P15151 |
| 1 | Coat protein VP1 | protein | 288 | 0% helix, 0% strand | P03300 |
| 2 | Coat protein VP2 | protein | 268 | 0% helix, 0% strand | P03300 |
| 3 | Coat protein VP3 | protein | 235 | 0% helix, 0% strand | P03300 |
| 4 | Coat protein VP4 | protein | 62 | 0% helix, 0% strand | P03300 |
Ligands and binding sites
- MYR · Myristic acid · ion · chains 4
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 591 | 0.80 | 0.84 | 189 | empty |
| 2 | 462 | 0.79 | 0.85 | 136 | empty |
| 3 | 201 | 0.70 | 0.85 | 102 | empty |
| 4 | 232 | 0.64 | 0.81 | 72 | empty |
| 5 | 164 | 0.44 | 0.72 | 46 | empty |
Interfaces
12 interfaces between chains.
- S–T · 8118 Ų buried · 0 hydrogen bonds · protein-protein
- R–S · 7472 Ų buried · 0 hydrogen bonds · protein-protein
- R–T · 7286 Ų buried · 0 hydrogen bonds · protein-protein
- 1–3 · 558 Ų buried · 0 hydrogen bonds · protein-protein
- 1–2 · 421 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 P15151
- Every structure of UniProt P03300
- Elsewhere: RCSB PDB 1NN8 · PDBe 1NN8 · UniProt P15151 · UniProt P03300
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