Research workbench
X-ray structure of spop math domain (S119D) in complex with a 53BP1 peptide
Analyse X-ray structure of spop math domain (S119D) in complex with a 53BP1 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LIO
- Type
- protein
- Length
- 286 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Speckle-type poz protein; TP53-binding protein 1 peptide
- UniProt
- O43791, Q12888
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 3 distinct chains · 7% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Speckle-type poz protein | protein | 136 | 8% helix, 51% strand | O43791 |
| C | TP53-binding protein 1 peptide | protein | 7 | 0% helix, 14% strand | Q12888 |
| D | TP53-binding protein 1 peptide | protein | 7 | 0% helix, 14% strand | Q12888 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 221 | 0.50 | 0.76 | 45 | empty |
| 2 | 184 | 0.49 | 0.76 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 523 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 392 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 361 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7LIO · X-ray structure of SPOP MATH domain (S119D) in complex with a 53BP1 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- O43791 · AlphaFold monomer V2.0 prediction for speckle-type poz protein (O43791) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 O43791
- Every structure of UniProt Q12888
- Elsewhere: RCSB PDB 7LIO · PDBe 7LIO · UniProt O43791 · UniProt Q12888
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