Research workbench
The high-resolution structure of ytbp-YTAF1 identifies conserved and competing interaction surfaces in transcriptional activation
Analyse The high-resolution structure of ytbp-YTAF1 identifies conserved and competing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B0A
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P46677, P13393
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 237 | — | P46677, P13393 |
Compared structures
- 4B0A · The high-resolution structure of yTBP-yTAF1 identifies conserved and competing… · the same entry in another collection · chain A against A, TM-score 1.00
- P13393 · AlphaFold monomer V2.0 prediction for tata-box-binding protein (P13393) · a predicted model of the same protein · chain A against A, TM-score 0.77
- P46677 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 1… · a predicted model of the same protein · chain A against A, TM-score 0.27
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 P46677
- Every structure of UniProt P13393
- Elsewhere: RCSB PDB 4B0A · PDBe 4B0A · UniProt P46677 · UniProt P13393
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