Research workbench
Structure of 53BP1 tandem tudor domains with E1549P and D1550N mutations
Analyse Structure of 53BP1 tandem tudor domains with E1549P and D1550N mutations in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MY0
- Type
- protein
- Length
- 240 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TP53-binding protein 1
- UniProt
- Q12888
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TP53-binding protein 1 | protein | 122 | 14% helix, 52% strand | Q12888 |
| B | TP53-binding protein 1 | protein | 118 | 13% helix, 56% strand | Q12888 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 181 | 0.55 | 0.80 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 487 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6MY0 · Structure of 53BP1 Tandem Tudor domains with E1549P and D1550N mutations · 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 Q12888
- Elsewhere: RCSB PDB 6MY0 · PDBe 6MY0 · UniProt Q12888
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.