Research workbench
Solution structure of the novel identified uba-like domain in the N- terminal of human etea protein
Analyse Solution structure of the novel identified uba-like domain in the N- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DAM
- Type
- protein
- Length
- 67 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Etea protein
- UniProt
- Q96CS3
Structure
solution nmr · 1 distinct chain · 52% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Etea protein | protein | 67 | 52% helix, 0% strand | Q96CS3 |
Compared structures
- 2DAM · Solution Structure of the Novel Identified UBA-like Domain in the N-terminal of Human… · the same entry in another collection · chain A against A, TM-score 1.00
- Q96CS3 · AlphaFold monomer V2.0 prediction for fas-associated factor 2 (Q96CS3) · a predicted model of the same protein · chain A against A, TM-score 0.73
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 Q96CS3
- Elsewhere: RCSB PDB 2DAM · PDBe 2DAM · UniProt Q96CS3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.