Research workbench
AlphaFold monomer V2.0 prediction for pre-B-cell leukemia transcription factor 1 (P41778)
Analyse AlphaFold monomer V2.0 prediction for pre-B-cell leukemia transcription factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P41778
- Type
- protein
- Length
- 430 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x632101649E208e9BB842605138AfB7073cbac29F
- Molecule
- Pre-B-cell leukemia transcription factor 1
- UniProt
- P41778
- Pockets
- 4 · best druggability 0.41
Structure
1 distinct chain · 54% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pre-B-cell leukemia transcription factor 1 | protein | 430 | 54% helix, 0% strand | P41778 |
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 | 82 | 0.41 | 0.79 | 15 | empty |
| 2 | 73 | 0.40 | 0.79 | 17 | empty |
| 3 | 89 | 0.35 | 0.75 | 16 | empty |
| 4 | 54 | 0.26 | 0.73 | 13 | empty |
Compared structures
- 1LFU · NMR Solution Structure of the Extended PBX Homeodomain Bound to DNA · an experimental structure of the same protein · chain A against P, TM-score 0.17
- 1LFU · NMR solution structure of the extended pbx homeodomain bound to DNA · an experimental structure of the same protein · chain A against P, TM-score 0.17
- 1DU6 · Solution structure of the truncated pbx homeodomain · an experimental structure of the same protein · chain A against A, TM-score 0.12
- 1DU6 · Solution structure of the truncated pbx homeodomain · an experimental structure of the same protein · chain A against A, TM-score 0.12
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 P41778
- Elsewhere: UniProt P41778 · AlphaFold DB P41778
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