MolNFT v1 · #129365 · protein
Dissociation of biochemical and antiretroviral activities of integrase-ledgf allosteric inhibitors revealed by resistance of A125 polymorphic HIV-1
5OI3: “Dissociation of biochemical and antiretroviral activities of integrase-ledgf allosteric inhibitors revealed…”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #129365 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
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