Research workbench
Tandem tudor domain of 53BP1
Analyse Tandem tudor domain of 53BP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XNI
- Type
- protein
- Length
- 1,180 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor suppressor P53-binding protein 1
- UniProt
- Q12888
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Tumor suppressor P53-binding protein 1 | protein | 118 | 14% helix, 48% strand | Q12888 |
Pockets
11 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.73 | 0.99 | 21 | empty |
| 2 | 52 | 0.72 | 0.99 | 19 | empty |
| 3 | 57 | 0.72 | 0.98 | 20 | empty |
| 4 | 173 | 0.66 | 0.86 | 35 | empty |
| 5 | 170 | 0.65 | 0.86 | 36 | empty |
Interfaces
9 interfaces between chains.
- D–J · 1057 Ų buried · 16 hydrogen bonds · protein-protein
- H–I · 1057 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1055 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 1046 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 543 Ų buried · 10 hydrogen bonds · protein-protein
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 Q12888
- Elsewhere: RCSB PDB 1XNI · PDBe 1XNI · UniProt Q12888
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.