Research workbench
Rb pocket bound to E7 lxcxe motif
Analyse Rb pocket bound to E7 lxcxe motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GUX
- Type
- protein
- Length
- 327 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoblastoma protein; Oncoprotein
- UniProt
- P06400
- Pockets
- 3 · best druggability 0.42
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoblastoma protein | protein | 177 | 77% helix, 0% strand | P06400 |
| B | Retinoblastoma protein | protein | 141 | 64% helix, 3% strand | P06400 |
| E | Oncoprotein | protein | 9 | 0% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.42 | 0.74 | 20 | empty |
| 2 | 64 | 0.32 | 0.75 | 13 | empty |
| 3 | 55 | 0.27 | 0.73 | 10 | empty |
Interfaces
2 interfaces between chains.
- A–B · 987 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 580 Ų buried · 7 hydrogen bonds · protein-protein
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 P06400
- Elsewhere: RCSB PDB 1GUX · PDBe 1GUX · UniProt P06400
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