MolNFT v1 · #48198 · protein
Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus
2PLV · Human poliovirus type 1 (subunit VP1): “Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus”. X-ray diffraction, 2 ligands (SPH, MYR), 10 pockets (best druggability 0.79). MolNFT…
- PDB
- 2PLV
- Type
- protein
- Length
- 853 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human poliovirus type 1 (subunit VP1); Human poliovirus type 1 (subunit VP2); Human…
- UniProt
- P03300
- Ligands
- SPH, MYR
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 11% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Human poliovirus type 1 (subunit VP1) | protein | 288 | 10% helix, 31% strand | P03300 |
| 2 | Human poliovirus type 1 (subunit VP2) | protein | 268 | 13% helix, 38% strand | P03300 |
| 3 | Human poliovirus type 1 (subunit VP3) | protein | 235 | 10% helix, 30% strand | P03300 |
| 4 | Human poliovirus type 1 (subunit VP4) | protein | 62 | 11% helix, 16% strand | P03300 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 637 | 0.79 | 0.84 | 93 | SPH |
| 2 | 133 | 0.45 | 0.77 | 28 | empty |
| 3 | 66 | 0.45 | 0.82 | 15 | empty |
| 4 | 140 | 0.44 | 0.76 | 33 | empty |
| 5 | 184 | 0.42 | 0.73 | 28 | empty |
Interfaces
6 interfaces between chains.
- 1–3 · 3992 Ų buried · 71 hydrogen bonds · protein-protein
- 1–2 · 2441 Ų buried · 40 hydrogen bonds · protein-protein
- 2–3 · 1680 Ų buried · 22 hydrogen bonds · protein-protein
- 1–4 · 1425 Ų buried · 26 hydrogen bonds · protein-protein
- 3–4 · 868 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 2PLV · Structural factors that control conformational transitions and serotype specificity in… · the same entry in another collection · chain 2 against 2, 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 P03300
- Elsewhere: RCSB PDB 2PLV · PDBe 2PLV · UniProt P03300
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