Research workbench
Structure of the DNA binding domains of nfat and FOXP2 bound specifically to DNA.
Analyse Structure of the DNA binding domains of nfat and FOXP2 bound specifically to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AS5
- Type
- protein + DNA
- Length
- 824 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q13469, O15409
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | dna | 21 | — | — |
| B, D | — | dna | 21 | — | — |
| N, M | — | protein | 287 | — | Q13469 |
| F, G | — | protein | 83 | — | O15409 |
Compared structures
- 2AS5 · Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA. · the same entry in another collection · chain G against G, TM-score 1.00
- O15409 · AlphaFold monomer V2.0 prediction for forkhead box protein P2 (O15409) · a predicted model of the same protein · chain F against A, TM-score 0.97
- Q13469 · AlphaFold monomer V2.0 prediction for nuclear factor of activated T-cells, cytoplasmic 2… · a predicted model of the same protein · chain N against A, TM-score 0.66
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 Q13469
- Every structure of UniProt O15409
- Elsewhere: RCSB PDB 2AS5 · PDBe 2AS5 · UniProt Q13469 · UniProt O15409
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