Research workbench
Crystal structure of transcription factor wer in complex with EGL3
Analyse Crystal structure of transcription factor wer in complex with EGL3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FDN
- Type
- protein
- Length
- 340 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor EGL1
- UniProt
- Q9CAD0
- Ligands
- NA, SO4, CL
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription factor EGL1 | protein | 169 | 41% helix, 21% strand | Q9CAD0 |
| B | Transcription factor EGL1 | protein | 171 | 40% helix, 21% strand | Q9CAD0 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains B
- GOL · Glycerol · additive · 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 | 131 | 0.59 | 0.84 | 16 | GOL |
Interfaces
1 interface between chains.
- A–B · 780 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7FDN · Crystal structure of transcription factor WER in complex with EGL3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9CAD0 · AlphaFold monomer V2.0 prediction for transcription factor EGL1 (Q9CAD0) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9CAD0
- Elsewhere: RCSB PDB 7FDN · PDBe 7FDN · UniProt Q9CAD0
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