Research workbench
Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-dp
Analyse Structural basis of DNA recognition by the heterodimeric cell cycle… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CF7
- Type
- protein + DNA
- Length
- 179 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16254, Q14188
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | dna | 15 | — | — |
| D | — | dna | 15 | — | — |
| A | — | protein | 67 | — | Q16254 |
| B | — | protein | 82 | — | Q14188 |
Compared structures
- 1CF7 · Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor… · the same entry in another collection · chain D against D, TM-score 1.00
- Q14188 · AlphaFold monomer V2.0 prediction for transcription factor dp-2 (Q14188) · a predicted model of the same protein · chain B against A, TM-score 0.95
- Q16254 · AlphaFold monomer V2.0 prediction for transcription factor E2F4 (Q16254) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q16254
- Every structure of UniProt Q14188
- Elsewhere: RCSB PDB 1CF7 · PDBe 1CF7 · UniProt Q16254 · UniProt Q14188
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