MolNFT v1 · #70916 · protein
Human early B-cell factor 1 (EBF1) DNA-binding domain
3LYR · Transcription factor COE1: “Human early B-cell factor 1 (EBF1) DNA-binding domain”. X-ray diffraction, 3 ligands (ZN, SO4, NH4), 1 pocket (best druggability 0.29). MolNFT v1 #70916 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3LYR
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor COE1
- UniProt
- Q9UH73
- Ligands
- ZN, SO4, NH4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription factor COE1 | protein | 211 | 12% helix, 39% strand | Q9UH73 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- NH4 · Ammonium ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.29 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
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 Q9UH73
- Elsewhere: RCSB PDB 3LYR · PDBe 3LYR · UniProt Q9UH73
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