Research workbench
AlphaFold monomer V2.0 prediction for nuclear factor of activated T-cells, cytoplasmic 1 (O95644)
Analyse AlphaFold monomer V2.0 prediction for nuclear factor of activated T-cells… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O95644
- Type
- protein
- Length
- 943 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa130963659F9ADED1C735201Bb05F57675e205B8
- Molecule
- Nuclear factor of activated T-cells, cytoplasmic 1
- UniProt
- O95644
- Pockets
- 4 · best druggability 0.42
Structure
1 distinct chain · 4% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear factor of activated T-cells, cytoplasmic 1 | protein | 943 | 4% helix, 14% strand | O95644 |
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 | 135 | 0.42 | 0.75 | 17 | empty |
| 2 | 75 | 0.32 | 0.74 | 13 | empty |
| 3 | 54 | 0.30 | 0.76 | 18 | empty |
| 4 | 54 | 0.26 | 0.73 | 12 | empty |
Compared structures
- 1A66 · Solution NMR structure of the core NFATC1/DNA complex, 18 structures · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 1A66 · Solution NMR structure of the core NFATC1/DNA complex, 18 structures · an experimental structure of the same protein · chain A against A, TM-score 0.17
- 1NFA · Human transcription factor nfatc DNA binding domain, NMR, 10 structures · an experimental structure of the same protein · chain A against A, TM-score 0.15
- 1NFA · Human transcription factor nfatc DNA binding domain, NMR, 10 structures · an experimental structure of the same protein · chain A against A, TM-score 0.15
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 O95644
- Elsewhere: UniProt O95644 · AlphaFold DB O95644
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