Research workbench
HIV-1 protease with mutation L76V in complex with grl-0519 (tris- tetrahydrofuran as P2 ligand)
Analyse HIV-1 protease with mutation L76V in complex with grl-0519 (tris… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DJ5
- Type
- protein
- Length
- 198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5RZ08
- Ligands
- G52, NA, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 99 | — | Q5RZ08 |
Ligands and binding sites
- G52 · (3r,3as,3br,6as,7as)-octahydrodifuro[2,3-B:3',2'-d]furan-3-yl [(1S,2R)-1-benzyl-2-hydroxy-3-{[(4-methoxyphenyl)sulfonyl](2-methylpropyl) amino}propyl]carbamate · ligand · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 5 copies · chains A, B
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DJ5 · HIV-1 protease with mutation L76V in complex with GRL-0519 (tris-tetrahydrofuran as P2… · 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 Q5RZ08
- Elsewhere: RCSB PDB 6DJ5 · PDBe 6DJ5 · UniProt Q5RZ08
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