Research workbench
Human foamy virus integrase - catalytic core.
Analyse Human foamy virus integrase - catalytic core. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X74
- Type
- protein
- Length
- 1,094 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Integrase
- UniProt
- P14350
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 6 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrase | protein | 187 | 39% helix, 16% strand | P14350 |
| B | Integrase | protein | 186 | 40% helix, 17% strand | P14350 |
| C | Integrase | protein | 178 | 40% helix, 19% strand | P14350 |
| D | Integrase | protein | 177 | 40% helix, 17% strand | P14350 |
| E | Integrase | protein | 186 | 39% helix, 17% strand | P14350 |
| F | Integrase | protein | 180 | 39% helix, 17% strand | P14350 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.73 | 0.98 | 22 | empty |
| 2 | 52 | 0.71 | 0.98 | 24 | empty |
| 3 | 55 | 0.71 | 0.97 | 22 | empty |
| 4 | 153 | 0.70 | 0.89 | 28 | empty |
| 5 | 177 | 0.69 | 0.87 | 33 | empty |
Interfaces
6 interfaces between chains.
- E–F · 1684 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1629 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1561 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 719 Ų buried · 2 hydrogen bonds · protein-protein
- C–F · 293 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 2X74 · Human foamy virus integrase - catalytic core. · 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 P14350
- Elsewhere: RCSB PDB 2X74 · PDBe 2X74 · UniProt P14350
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