Research workbench
Conformational isomerism of endothelin in acidic aqueous media: a quantitative noesy analysis
Analyse Conformational isomerism of endothelin in acidic aqueous media: a quantitative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EDP
- Type
- protein
- Length
- 17 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothelin-1 precursor
- UniProt
- P05305
Structure
solution nmr · 1 distinct chain · 41% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endothelin-1 precursor | protein | 17 | 41% helix, 0% strand | P05305 |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1EDP · Conformational isomerism of endothelin in acidic aqueous media: a quantitative noesy… · the same entry in another collection · chain A against A, TM-score 1.00
- P05305 · AlphaFold monomer V2.0 prediction for endothelin-1 (P05305) · a predicted model of the same protein · chain A against A, TM-score 0.30
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 P05305
- Elsewhere: RCSB PDB 1EDP · PDBe 1EDP · UniProt P05305
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