MolNFT v1 · #129366 · protein
Dissociation of biochemical and antiretroviral activities of integrase-ledgf allosteric inhibitors revealed by resistance of A125 polymorphic HIV-1
5OI5: “Dissociation of biochemical and antiretroviral activities of integrase-ledgf allosteric inhibitors revealed…”. X-ray diffraction, 2 ligands (9VK, MG). MolNFT v1 #129366 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OI5
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0U2K7W4
- Ligands
- 9VK, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 131 | — | A0A0U2K7W4 |
Ligands and binding sites
- 9VK · (2~{S})-2-[4-(4,4-dimethylcyclohexen-1-yl)-2-methyl-5-pyridin-2-yl-thiophen-3-yl]-2-[(2-methylpropan-2-yl)oxy]ethanoic acid · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OI5 · Dissociation of biochemical and antiretroviral activities of Integrase-LEDGF Allosteric… · 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 A0A0U2K7W4
- Elsewhere: RCSB PDB 5OI5 · PDBe 5OI5 · UniProt A0A0U2K7W4
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