Research workbench
Crystal structure of TOPBP1 BRCT7/8
Analyse Crystal structure of TOPBP1 BRCT7/8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AL2
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA topoisomerase 2-binding protein 1
- UniProt
- Q92547
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA topoisomerase 2-binding protein 1 | protein | 220 | 46% helix, 14% strand | Q92547 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.38 | 0.75 | 20 | empty |
| 2 | 52 | 0.28 | 0.74 | 12 | empty |
Modifications
Observed in the structure: 2 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 Q92547
- Elsewhere: RCSB PDB 3AL2 · PDBe 3AL2 · UniProt Q92547
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