Research workbench
Crystal structure of the 53BP1 tandem tudor domain in complex with P53K370ME2
Analyse Crystal structure of the 53BP1 tandem tudor domain in complex with P53K370ME2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LGF
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor suppressor P53-binding protein 1
- UniProt
- Q12888
- Ligands
- MLY, SO4
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor suppressor P53-binding protein 1 | protein | 119 | 13% helix, 54% strand | Q12888 |
Ligands and binding sites
- MLY · N-dimethyl-lysine · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- PGE · Triethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3LGF · Crystal structure of the 53BP1 tandem tudor domain in complex with p53K370me2 · 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 0.97
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 3LGF · PDBe 3LGF · UniProt Q12888
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