Research workbench
HIV-1 protease wt (NL4-3) in complex with PU8 (LR4-06)
Analyse HIV-1 protease wt (NL4-3) in complex with PU8 (LR4-06) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LEG
- Type
- protein
- Length
- 198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8ULI9
- Ligands
- XVY, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | — | protein | 99 | — | Q8ULI9 |
Ligands and binding sites
- XVY · Diethyl [(4-{(2S,3R)-4-[(2-ethylbutyl){[4-(hydroxymethyl)phenyl]sulfonyl}amino]-2-[({[(3r,3as, 6AR)-hexahydrofuro[2,3-b]furan-3-yl]oxy}carbonyl) amino]-3-hydroxybutyl}phenoxy)methyl]phosphonate · ligand · chains B, A
- SO4 · Sulfate ion · ion · 5 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LEG · HIV-1 Protease WT (NL4-3) in Complex with PU8 (LR4-06) · 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 7LEG · PDBe 7LEG · UniProt Q8ULI9
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