Research workbench
Dual inhibition of HIV-1 replication by integrase-ledgf allosteric inhibitors is predominant at post-integration stage during virus production rather than at integration
Analyse Dual inhibition of HIV-1 replication by integrase-ledgf allosteric inhibitors… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LH4
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Integrase
- UniProt
- Q9WJM2
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrase | protein | 131 | 50% helix, 22% strand | Q9WJM2 |
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
- 4LH4 · Dual inhibition of HIV-1 replication by Integrase-LEDGF allosteric inhibitors is… · 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 Q9WJM2
- Elsewhere: RCSB PDB 4LH4 · PDBe 4LH4 · UniProt Q9WJM2
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