Research workbench
HMGB1-facilitated P53 DNA binding occurs via hmg-BOX/P53 transactivation domain interaction and is regulated by the acidic tail
Analyse HMGB1-facilitated P53 DNA binding occurs via hmg-BOX/P53 transactivation domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LY4
- Type
- protein
- Length
- 130 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High mobility group protein B1; Cellular tumor antigen P53
- UniProt
- P09429, P04637
- Pockets
- 1 · best druggability 0.41
Structure
solution nmr · 2 distinct chains · 43% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High mobility group protein B1 | protein | 83 | 63% helix, 0% strand | P09429 |
| B | Cellular tumor antigen P53 | protein | 47 | 9% helix, 0% strand | P04637 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.41 | 0.73 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 815 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2LY4 · HMGB1-facilitated p53 DNA binding occurs via HMG-box/p53 transactivation domain… · the same entry in another collection · chain A against A, TM-score 1.00
- P09429 · AlphaFold monomer V2.0 prediction for high mobility group protein B1 (P09429) · a predicted model of the same protein · chain A against A, TM-score 0.69
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 P09429
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 2LY4 · PDBe 2LY4 · UniProt P09429 · UniProt P04637
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