Research workbench
HIV-1 protease NL4-3 wt in complex with lr-100
Analyse HIV-1 protease NL4-3 wt in complex with lr-100 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OXW
- Type
- protein
- Length
- 198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease NL4-3
- UniProt
- Q8ULI9
- Ligands
- NFJ
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Protease NL4-3 | protein | 99 | 4% helix, 58% strand | Q8ULI9 |
Ligands and binding sites
- NFJ · (3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-yl {(2S,3R)-4-[(2-ethylbutyl)({4-[(1R)-1-hydroxyethyl]phenyl}sulfonyl)amino]-3-hydroxy-1-phenylbutan-2-yl}carbamate · ligand · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 411 | 0.71 | 0.82 | 36 | NFJ |
Interfaces
1 interface between chains.
- B–A · 1848 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 6OXW · HIV-1 Protease NL4-3 WT in Complex with LR-100 · the same entry in another collection · chain B against B, 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 Q8ULI9
- Elsewhere: RCSB PDB 6OXW · PDBe 6OXW · UniProt Q8ULI9
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