Research workbench
AlphaFold monomer V2.0 prediction for protein disulfide isomerase- like 1-2 (Q9SRG3)
Analyse AlphaFold monomer V2.0 prediction for protein disulfide isomerase- like 1-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9SRG3
- Type
- protein
- Length
- 508 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf96C5834Ad687e9EbeF5b6A56c77eb1420b55e4A
- Molecule
- Protein disulfide isomerase-like 1-2
- UniProt
- Q9SRG3
- Pockets
- 4 · best druggability 0.50
Structure
1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein disulfide isomerase-like 1-2 | protein | 508 | 32% helix, 19% strand | Q9SRG3 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.50 | 0.76 | 28 | empty |
| 2 | 146 | 0.43 | 0.75 | 21 | empty |
| 3 | 76 | 0.38 | 0.78 | 14 | empty |
| 4 | 54 | 0.30 | 0.75 | 10 | empty |
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 Q9SRG3
- Elsewhere: UniProt Q9SRG3 · AlphaFold DB Q9SRG3
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