Research workbench
Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide
Analyse Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O9K
- Type
- protein
- Length
- 1,424 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoblastoma-associated protein; Transcription factor E2F1
- UniProt
- P06400, Q01094
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 65% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Retinoblastoma-associated protein | protein | 194 | 72% helix, 0% strand | P06400 |
| B, D, F, H | Retinoblastoma-associated protein | protein | 144 | 63% helix, 3% strand | P06400 |
| P, Q, R, S | Transcription factor E2F1 | protein | 18 | 22% helix, 0% strand | Q01094 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1014 | 0.82 | 0.83 | 73 | empty |
| 2 | 908 | 0.79 | 0.81 | 90 | empty |
| 3 | 364 | 0.64 | 0.80 | 29 | empty |
| 4 | 67 | 0.60 | 0.90 | 18 | empty |
| 5 | 273 | 0.59 | 0.79 | 27 | empty |
Interfaces
23 interfaces between chains.
- A–E · 1228 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1036 Ų buried · 12 hydrogen bonds · protein-protein
- G–H · 1019 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 1015 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1011 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1O9K · Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide · the same entry in another collection · chain S against S, TM-score 1.00
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 P06400
- Every structure of UniProt Q01094
- Elsewhere: RCSB PDB 1O9K · PDBe 1O9K · UniProt P06400 · UniProt Q01094
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