Research workbench
AlphaFold monomer V2.0 prediction for SAM pointed domain-containing ets transcription factor (O95238)
Analyse AlphaFold monomer V2.0 prediction for SAM pointed domain-containing ets… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O95238
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc7B07e4CAc3aef57E90cd1aaf9cfB5A071144eAF
- Molecule
- SAM pointed domain-containing ets transcription factor
- UniProt
- O95238
- Pockets
- 2 · best druggability 0.53
Structure
1 distinct chain · 38% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SAM pointed domain-containing ets transcription factor | protein | 335 | 38% helix, 4% strand | O95238 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 224 | 0.53 | 0.77 | 33 | empty |
| 2 | 138 | 0.41 | 0.74 | 16 | empty |
Compared structures
- 1YO5 · Analysis of the 2.0A crystal structure of the protein-DNA complex of human PDEF Ets… · an experimental structure of the same protein · chain A against C, TM-score 0.26
- 1YO5 · Analysis of the 2.0A crystal structure of the protein-DNA complex of human pdef ets… · an experimental structure of the same protein · chain A against C, TM-score 0.26
- 2DKX · Solution structure of the SAM_PNT-domain of ETS transcription factor PDEF (Prostate ets) · an experimental structure of the same protein · chain A against A, TM-score 0.26
- 2DKX · Solution structure of the SAM_PNT-domain of ets transcription factor pdef (prostate ets) · an experimental structure of the same protein · chain A against A, TM-score 0.26
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 O95238
- Elsewhere: UniProt O95238 · AlphaFold DB O95238
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