Research workbench
Topoisomerase VI-B, ADP-bound monomer form
Analyse Topoisomerase VI-B, ADP-bound monomer form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z59
- Type
- protein
- Length
- 462 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type II DNA topoisomerase VI subunit B
- EC
- 5.99.1.3
- UniProt
- O05207
- Ligands
- ADP, MG
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type II DNA topoisomerase VI subunit B (EC 5.99.1.3) | protein | 462 | 39% helix, 23% strand | O05207 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 732 | 0.70 | 0.76 | 55 | MG, ADP |
| 2 | 62 | 0.33 | 0.76 | 15 | empty |
| 3 | 61 | 0.29 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
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 O05207
- Elsewhere: RCSB PDB 1Z59 · PDBe 1Z59 · UniProt O05207
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