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Topoisomerase residues 410-1202,
Analyse Topoisomerase residues 410-1202, in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BGW
- Type
- protein
- Length
- 679 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Topoisomerase
- UniProt
- P06786
- Pockets
- 7 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Topoisomerase | protein | 679 | 43% helix, 15% strand | P06786 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 472 | 0.66 | 0.78 | 38 | empty |
| 2 | 430 | 0.65 | 0.78 | 33 | empty |
| 3 | 216 | 0.54 | 0.78 | 23 | empty |
| 4 | 166 | 0.47 | 0.76 | 28 | empty |
| 5 | 173 | 0.46 | 0.75 | 32 | empty |
Compared structures
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 P06786
- Elsewhere: RCSB PDB 1BGW · PDBe 1BGW · UniProt P06786
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