Research workbench
P107 pocket domain complexed with EID1 peptide
Analyse P107 pocket domain complexed with EID1 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SMD
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoblastoma-like protein 1; EP300-interacting inhibitor of differentiation 1
- UniProt
- P28749, Q9Y6B2
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoblastoma-like protein 1 | protein | 342 | 67% helix, 2% strand | P28749 |
| B | EP300-interacting inhibitor of differentiation 1 | protein | 14 | 0% helix, 0% strand | Q9Y6B2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.40 | 0.75 | 20 | empty |
| 2 | 61 | 0.25 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 673 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 7SMD · p107 pocket domain complexed with EID1 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P28749 · AlphaFold monomer V2.0 prediction for retinoblastoma-like protein 1 (P28749) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9Y6B2 · AlphaFold monomer V2.0 prediction for EP300-interacting inhibitor of differentiation 1… · a predicted model of the same protein · chain B against A, TM-score 0.23
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 P28749
- Every structure of UniProt Q9Y6B2
- Elsewhere: RCSB PDB 7SMD · PDBe 7SMD · UniProt P28749 · UniProt Q9Y6B2
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