Research workbench
Dissociation of biochemical and antiretroviral activities of integrase-ledgf allosteric inhibitors revealed by resistance of A125 polymorphic HIV-1
Analyse Dissociation of biochemical and antiretroviral activities of integrase-ledgf… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OI3
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Integrase
- UniProt
- B9VID1
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrase | protein | 131 | 52% helix, 22% strand | B9VID1 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (artifact).
Compared structures
- 5OI3 · 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 B9VID1
- Elsewhere: RCSB PDB 5OI3 · PDBe 5OI3 · UniProt B9VID1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.