Research workbench
P107 pocket domain in complex with LIN52 P29A peptide
Analyse P107 pocket domain in complex with LIN52 P29A peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YOO
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoblastoma-like protein 1,RETINOBLASTOMA-like protein 1; LIN52 peptide
- UniProt
- P28749
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoblastoma-like protein 1,RETINOBLASTOMA-like protein 1 | protein | 343 | 63% helix, 1% strand | P28749 |
| X | LIN52 peptide | protein | 18 | 22% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 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 | 143 | 0.44 | 0.75 | 23 | empty |
| 2 | 94 | 0.33 | 0.73 | 23 | empty |
Interfaces
1 interface between chains.
- A–X · 753 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
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 P28749
- Elsewhere: RCSB PDB 4YOO · PDBe 4YOO · UniProt P28749
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