Research workbench
AlphaFold monomer V2.0 prediction for zinc finger E-box-binding homeobox protein zag-1 (G5EBU4)
Analyse AlphaFold monomer V2.0 prediction for zinc finger E-box-binding homeobox… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- G5EBU4
- Type
- protein
- Length
- 596 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7Be92d8bdcB542e761fbcA406db9F1e2Df9F8F8C
- Molecule
- Zinc finger E-box-binding homeobox protein zag-1
- UniProt
- G5EBU4
- Pockets
- 3 · best druggability 0.60
Structure
1 distinct chain · 29% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger E-box-binding homeobox protein zag-1 | protein | 596 | 29% helix, 4% strand | G5EBU4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 333 | 0.60 | 0.77 | 32 | empty |
| 2 | 117 | 0.40 | 0.75 | 17 | empty |
| 3 | 56 | 0.29 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 G5EBU4
- Elsewhere: UniProt G5EBU4 · AlphaFold DB G5EBU4
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