Research workbench
AlphaFold monomer V2.0 prediction for obg-like ATPase homolog (P38746)
Analyse AlphaFold monomer V2.0 prediction for obg-like ATPase homolog (P38746) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P38746
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Obg-like ATPase homolog
- UniProt
- P38746
- Pockets
- 5 · best druggability 0.64
Structure
1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Obg-like ATPase homolog | protein | 405 | 44% helix, 18% strand | P38746 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.64 | 0.88 | 20 | empty |
| 2 | 262 | 0.59 | 0.78 | 35 | empty |
| 3 | 97 | 0.46 | 0.80 | 16 | empty |
| 4 | 101 | 0.36 | 0.75 | 18 | empty |
| 5 | 66 | 0.26 | 0.72 | 19 | 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 P38746
- Elsewhere: UniProt P38746 · AlphaFold DB P38746
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