Research workbench
Solution structure of 53BP1 tandem tudor domains in complex with a P53K370ME2 peptide
Analyse Solution structure of 53BP1 tandem tudor domains in complex with a P53K370ME2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MWO
- Type
- protein
- Length
- 138 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor suppressor P53-binding protein 1; Cellular tumor antigen P53
- UniProt
- Q12888, P04637
Structure
solution nmr · 2 distinct chains · 12% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor suppressor P53-binding protein 1 | protein | 123 | 14% helix, 52% strand | Q12888 |
| B | Cellular tumor antigen P53 | protein | 15 | 0% helix, 0% strand | P04637 |
Interfaces
1 interface between chains.
- A–B · 732 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 2MWO · Solution structure of 53BP1 tandem Tudor domains in complex with a p53K370me2 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q12888 · AlphaFold monomer V2.0 prediction for TP53-binding protein 1 (Q12888) · a predicted model of the same protein · chain A against A, TM-score 0.84
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
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 2MWO · PDBe 2MWO · UniProt Q12888 · UniProt P04637
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