Research workbench
GP41-targeting HIV-1 fusion inhibitors with helical ile-asp-leu tail
Analyse GP41-targeting HIV-1 fusion inhibitors with helical ile-asp-leu tail in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HFL
- Type
- protein
- Length
- 413 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope GLYCOPROTEIN,GP41 chr region
- UniProt
- A1YNW7
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 5 distinct chains · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | Envelope GLYCOPROTEIN,GP41 chr region | protein | 69 | 87% helix, 0% strand | A1YNW7 |
| B | Envelope GLYCOPROTEIN,GP41 chr region | protein | 71 | 86% helix, 0% strand | A1YNW7 |
| C | Envelope GLYCOPROTEIN,GP41 chr region | protein | 70 | 83% helix, 0% strand | A1YNW7 |
| D | Envelope GLYCOPROTEIN,GP41 chr region | protein | 69 | 87% helix, 0% strand | A1YNW7 |
| E | Envelope GLYCOPROTEIN,GP41 chr region | protein | 65 | 91% helix, 0% strand | A1YNW7 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.41 | 0.78 | 11 | empty |
Interfaces
8 interfaces between chains.
- A–C · 1343 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1307 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 1293 Ų buried · 12 hydrogen bonds · protein-protein
- D–F · 1266 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 1255 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5HFL · Gp41-targeting HIV-1 fusion inhibitors with helical Ile-Asp-Leu tail · 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 A1YNW7
- Elsewhere: RCSB PDB 5HFL · PDBe 5HFL · UniProt A1YNW7
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