Research workbench
Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases
Analyse Crystal structure of the catalytic domain of HIV-1 integrase: similarity to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ITG
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV-1 integrase
- UniProt
- P12497
- Ligands
- CAC
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HIV-1 integrase | protein | 142 | 44% helix, 20% strand | P12497 |
Ligands and binding sites
- CAC · Cacodylate ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1ITG · Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other… · 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 1ITG · PDBe 1ITG · UniProt P12497
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.