Research workbench
AlphaFold monomer V2.0 prediction for zwei ig domain protein zig-1 (G5EGI7)
Analyse AlphaFold monomer V2.0 prediction for zwei ig domain protein zig-1 (G5EGI7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- G5EGI7
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x166774432Fa02840CA63277F9d861DcB92479204
- Molecule
- Zwei ig domain protein zig-1
- UniProt
- G5EGI7
- Pockets
- 2 · best druggability 0.52
Structure
1 distinct chain · 13% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zwei ig domain protein zig-1 | protein | 265 | 13% helix, 40% strand | G5EGI7 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 139 | 0.52 | 0.80 | 24 | empty |
| 2 | 61 | 0.28 | 0.73 | 17 | 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 G5EGI7
- Elsewhere: UniProt G5EGI7 · AlphaFold DB G5EGI7
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