Research workbench
Human transcription factor nfatc DNA binding domain, NMR, 10 structures
Analyse Human transcription factor nfatc DNA binding domain, NMR, 10 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NFA
- Type
- protein
- Length
- 178 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human transcription factor NFATC1
- UniProt
- O95644
- Pockets
- 2 · best druggability 0.75
Structure
solution nmr · 1 distinct chain · 2% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human transcription factor NFATC1 | protein | 178 | 2% helix, 24% strand | O95644 |
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 | 302 | 0.75 | 0.87 | 64 | empty |
| 2 | 58 | 0.26 | 0.73 | 16 | empty |
Compared structures
- 1NFA · Human transcription factor nfatc DNA binding domain, NMR, 10 structures · the same entry in another collection · chain A against A, TM-score 1.00
- O95644 · AlphaFold monomer V2.0 prediction for nuclear factor of activated T-cells, cytoplasmic 1… · a predicted model of the same protein · chain A against A, TM-score 0.65
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: RCSB PDB 1NFA · PDBe 1NFA · UniProt O95644
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