Research workbench
Solution structure of conotoxin Y-piiie from conus purpurascens, NMR, 14 structures
Analyse Solution structure of conotoxin Y-piiie from conus purpurascens, NMR, 14… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AS5
- Type
- protein
- Length
- 24 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conotoxin Y-piiie
- UniProt
- P56529
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conotoxin Y-piiie | protein | 24 | 0% helix, 0% strand | P56529 |
Ligands and binding sites
- NH2 · Amino group · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 3 modified (disulfide, hydroxylation).
Compared structures
- 1AS5 · Solution structure of conotoxin Y-piiie from conus purpurascens, NMR, 14 structures · the same entry in another collection · chain A against A, TM-score 1.00
- P56529 · AlphaFold monomer V2.0 prediction for psi-conotoxin piiie (P56529) · a predicted model of the same protein · chain A against A, TM-score 0.20
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 P56529
- Elsewhere: RCSB PDB 1AS5 · PDBe 1AS5 · UniProt P56529
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