Research workbench
AlphaFold monomer V2.0 prediction for protein disulfide-isomerase A4 (Q29RV1)
Analyse AlphaFold monomer V2.0 prediction for protein disulfide-isomerase A4 (Q29RV1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q29RV1
- Type
- protein
- Length
- 643 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Protein disulfide-isomerase A4
- UniProt
- Q29RV1
- Pockets
- 4 · best druggability 0.56
Structure
1 distinct chain · 30% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein disulfide-isomerase A4 | protein | 643 | 30% helix, 19% strand | Q29RV1 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 347 | 0.56 | 0.75 | 37 | empty |
| 2 | 113 | 0.42 | 0.77 | 19 | empty |
| 3 | 91 | 0.36 | 0.75 | 15 | empty |
| 4 | 62 | 0.26 | 0.72 | 18 | 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 Q29RV1
- Elsewhere: UniProt Q29RV1 · AlphaFold DB Q29RV1
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