Research workbench
HIV-1 integrase catalytic core domain A128T mutant complexed with allosteric inhibitor
Analyse HIV-1 integrase catalytic core domain A128T mutant complexed with allosteric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GVM
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gag-pol polyprotein
- EC
- 3.4.23.16, 2.7.7.49, 2.7.7.7, 3.1.26.13, 3.1.13.2
- UniProt
- P12497
- Ligands
- LF2, ARS
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gag-pol polyprotein (EC 3.4.23.16, 2.7.7.49, 2.7.7.7, 3.1.26.13, 3.1.13.2) | protein | 148 | 46% helix, 22% strand | P12497 |
Ligands and binding sites
- LF2 · (2S)-[6-bromo-4-(4-chlorophenyl)-2-methylquinolin-3-yl](tert-butoxy)ethanoic acid · ligand · chains A
- ARS · Arsenic · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4GVM · HIV-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor · 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 P12497
- Elsewhere: RCSB PDB 4GVM · PDBe 4GVM · UniProt P12497
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.