Research workbench
Crystal structure of the human TAF4-TAF12 (TAFII135-TAFII20) complex
Analyse Crystal structure of the human TAF4-TAF12 (TAFII135-TAFII20) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H3O
- Type
- protein
- Length
- 246 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O00268, Q16514
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 49 | — | O00268 |
| B, D | — | protein | 74 | — | Q16514 |
Compared structures
- 1H3O · Crystal Structure of the Human TAF4-TAF12 (TAFII135-TAFII20) Complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q16514 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 12… · a predicted model of the same protein · chain B against A, TM-score 0.95
- 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 0.83
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
- Every structure of UniProt Q16514
- Elsewhere: RCSB PDB 1H3O · PDBe 1H3O · UniProt O00268 · UniProt Q16514
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.