Research workbench
Structure of 53BP1/METHYLATED histone peptide complex
Analyse Structure of 53BP1/METHYLATED histone peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IG0
- Type
- protein
- Length
- 121 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor suppressor P53-binding protein 1; Dimethylated histone H4-K20 peptide
- UniProt
- Q12888
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor suppressor P53-binding protein 1 | protein | 119 | 13% helix, 54% strand | Q12888 |
| B | Dimethylated histone H4-K20 peptide | protein | 2 | 0% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 98 | 0.37 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 275 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
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 2IG0 · PDBe 2IG0 · UniProt Q12888
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