Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein htpg (A1T639)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein htpg (A1T639) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1T639
- Type
- protein
- Length
- 651 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF65fB8c570786E581ea9779106AdfF4278387288
- Molecule
- Chaperone protein htpg
- UniProt
- A1T639
- Pockets
- 9 · best druggability 0.76
Structure
1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein htpg | protein | 651 | 41% helix, 21% strand | A1T639 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 736 | 0.76 | 0.81 | 83 | empty |
| 2 | 109 | 0.74 | 0.95 | 29 | empty |
| 3 | 226 | 0.61 | 0.81 | 32 | empty |
| 4 | 171 | 0.50 | 0.78 | 26 | empty |
| 5 | 138 | 0.41 | 0.75 | 21 | 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 A1T639
- Elsewhere: UniProt A1T639 · AlphaFold DB A1T639
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