Research workbench
An oligomerization domain confers pioneer properties to the leafy master floral regulator
Analyse An oligomerization domain confers pioneer properties to the leafy master floral… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UDE
- Type
- protein
- Length
- 163 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ginlfy protein
- UniProt
- Q9LLY6
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ginlfy protein | protein | 85 | 73% helix, 0% strand | Q9LLY6 |
| B | Ginlfy protein | protein | 78 | 69% helix, 0% strand | Q9LLY6 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · chains A, B
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 | 96 | 0.36 | 0.74 | 19 | empty |
| 2 | 75 | 0.28 | 0.72 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 635 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4UDE · An oligomerization domain confers pioneer properties to the LEAFY master floral regulator · the same entry in another collection · chain A against A, 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 Q9LLY6
- Elsewhere: RCSB PDB 4UDE · PDBe 4UDE · UniProt Q9LLY6
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