Research workbench
Structure of tafh domain of the human TAF4 subunit of tfiid
Analyse Structure of tafh domain of the human TAF4 subunit of tfiid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P6V
- Type
- protein
- Length
- 97 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription initiation factor tfiid subunit 4
- UniProt
- O00268
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription initiation factor tfiid subunit 4 | protein | 97 | 72% helix, 0% strand | O00268 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 8 modified (methylation).
Compared structures
- 2P6V · Structure of TAFH domain of the human TAF4 subunit of TFIID · the same entry in another collection · chain A against A, TM-score 1.00
- O00268 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 4… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O00268
- Elsewhere: RCSB PDB 2P6V · PDBe 2P6V · UniProt O00268
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