Research workbench
Catalytic domain of HIV-1 integrase
Analyse Catalytic domain of HIV-1 integrase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BI4
- Type
- protein
- Length
- 445 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Integrase
- UniProt
- P12497
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrase | protein | 142 | 41% helix, 23% strand | P12497 |
| B | Integrase | protein | 143 | 48% helix, 22% strand | P12497 |
| C | Integrase | protein | 160 | 44% helix, 22% strand | P12497 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.68 | 0.97 | 28 | empty |
| 2 | 209 | 0.53 | 0.78 | 30 | empty |
| 3 | 171 | 0.48 | 0.76 | 19 | empty |
| 4 | 126 | 0.46 | 0.78 | 18 | empty |
| 5 | 65 | 0.35 | 0.77 | 20 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1504 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 348 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1BI4 · Catalytic domain of HIV-1 integrase · 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 1BI4 · PDBe 1BI4 · UniProt P12497
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