Research workbench
Structure of the transmembrane domain of HIV-1 GP41 in bicelle
Analyse Structure of the transmembrane domain of HIV-1 GP41 in bicelle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JYN
- Type
- protein
- Length
- 120 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Envelope glycoprotein GP160
- UniProt
- Q74849
- Pockets
- 3 · best druggability 0.72
Structure
solution nmr · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Envelope glycoprotein GP160 | protein | 40 | 75% helix, 0% strand | Q74849 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.72 | 0.89 | 32 | empty |
| 2 | 157 | 0.69 | 0.88 | 15 | empty |
| 3 | 130 | 0.60 | 0.84 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 667 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 617 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 595 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5JYN · Structure of the transmembrane domain of HIV-1 gp41 in bicelle · 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 Q74849
- Elsewhere: RCSB PDB 5JYN · PDBe 5JYN · UniProt Q74849
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