Research workbench
NMR structure of the uba domain of S. cerevisiae DCN1
Analyse NMR structure of the uba domain of S. cerevisiae DCN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L4E
- Type
- protein
- Length
- 57 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Defective in cullin neddylation protein 1
- UniProt
- Q12395
Structure
solution nmr · 1 distinct chain · 40% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Defective in cullin neddylation protein 1 | protein | 57 | 40% helix, 0% strand | Q12395 |
Compared structures
- 2L4E · NMR structure of the UBA domain of S. cerevisiae Dcn1 · the same entry in another collection · chain A against A, 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 0.78
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
- Elsewhere: RCSB PDB 2L4E · PDBe 2L4E · UniProt Q12395
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.