Research workbench
Early B-cell factor 3 (EBF3) IPT/TIG and dimerization helices
Analyse Early B-cell factor 3 (EBF3) IPT/TIG and dimerization helices in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MUJ
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor COE3
- UniProt
- Q9H4W6
- Ligands
- CL
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transcription factor COE3 | protein | 133 | 20% helix, 38% strand | Q9H4W6 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.66 | 0.76 | 48 | CL, EDO |
Interfaces
1 interface between chains.
- A–B · 1678 Ų buried · 19 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 Q9H4W6
- Elsewhere: RCSB PDB 3MUJ · PDBe 3MUJ · UniProt Q9H4W6
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