Research workbench
Crystal structure of the CHP1-TAS3 complex core
Analyse Crystal structure of the CHP1-TAS3 complex core in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TIX
- Type
- protein
- Length
- 1,145 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q12306, O94687, Q10103
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 153 | — | Q12306, O94687 |
| B | — | protein | 421 | — | Q10103 |
| C | — | protein | 147 | — | Q12306, O94687 |
| D | — | protein | 424 | — | Q10103 |
Compared structures
- 3TIX · Crystal structure of the Chp1-Tas3 complex core · the same entry in another collection · chain D against D, TM-score 1.00
- Q10103 · AlphaFold monomer V2.0 prediction for chromo domain-containing protein 1 (Q10103) · a predicted model of the same protein · chain D against A, TM-score 0.99
- Q12306 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein SMT3 (Q12306) · a predicted model of the same protein · chain C against A, TM-score 0.51
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 Q12306
- Every structure of UniProt O94687
- Every structure of UniProt Q10103
- Elsewhere: RCSB PDB 3TIX · PDBe 3TIX · UniProt Q12306 · UniProt O94687 · UniProt Q10103
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