Research workbench
Yeast CUL1WHB-DCN1P acetylated UBC12N complex
Analyse Yeast CUL1WHB-DCN1P acetylated UBC12N complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TDI
- Type
- protein
- Length
- 427 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q12395, P52491
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 200 | — | Q12395 |
| A | — | protein | 202 | — | Q12395 |
| C | — | protein | 13 | — | P52491 |
| D | — | protein | 12 | — | P52491 |
Compared structures
- 3TDI · yeast Cul1WHB-Dcn1P acetylated Ubc12N complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q12395 · AlphaFold monomer V2.0 prediction for defective in cullin neddylation protein 1 (Q12395) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P52491 · AlphaFold monomer V2.0 prediction for NEDD8-conjugating enzyme UBC12 (P52491) · a predicted model of the same protein · chain D against A, TM-score 0.74
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 Q12395
- Every structure of UniProt P52491
- Elsewhere: RCSB PDB 3TDI · PDBe 3TDI · UniProt Q12395 · UniProt P52491
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.