Research workbench
P1/MAHONEY poliovirus, double mutant P1095S + H2142Y
Analyse P1/MAHONEY poliovirus, double mutant P1095S + H2142Y in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AR7
- Type
- protein
- Length
- 851 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P1/MAHONEY poliovirus
- UniProt
- P03300, P03299
- Ligands
- SPH, MYR
- Pockets
- 13 · best druggability 0.79
Structure
x-ray diffraction · 5 distinct chains · 11% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 0 | P1/MAHONEY poliovirus | protein | 5 | 0% helix, 60% strand | — |
| 1 | P1/MAHONEY poliovirus | protein | 283 | 10% helix, 32% strand | P03300 |
| 2 | P1/MAHONEY poliovirus | protein | 268 | 14% helix, 38% strand | P03300 |
| 3 | P1/MAHONEY poliovirus | protein | 235 | 9% helix, 30% strand | P03300 |
| 4 | P1/MAHONEY poliovirus | protein | 60 | 12% helix, 18% strand | P03299 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 660 | 0.79 | 0.83 | 82 | SPH |
| 2 | 128 | 0.45 | 0.78 | 27 | empty |
| 3 | 145 | 0.44 | 0.75 | 32 | empty |
| 4 | 192 | 0.43 | 0.73 | 27 | empty |
| 5 | 71 | 0.42 | 0.80 | 13 | empty |
Interfaces
7 interfaces between chains.
- 1–3 · 3947 Ų buried · 75 hydrogen bonds · protein-protein
- 1–2 · 2370 Ų buried · 38 hydrogen bonds · protein-protein
- 2–3 · 1659 Ų buried · 22 hydrogen bonds · protein-protein
- 1–4 · 1175 Ų buried · 17 hydrogen bonds · protein-protein
- 3–4 · 868 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 lipid (myristoylation).
Compared structures
- 1AR7 · P1/MAHONEY poliovirus, double mutant P1095S + H2142Y · 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
- Every structure of UniProt P03299
- Elsewhere: RCSB PDB 1AR7 · PDBe 1AR7 · UniProt P03300 · UniProt P03299
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