Research workbench
NMR solution structures of delta-conotoxin evia from conus ermineus that selectively acts on vertebrate neuronal na+ channels
Analyse NMR solution structures of delta-conotoxin evia from conus ermineus that… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G1P
- Type
- protein
- Length
- 32 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conotoxin evia
- UniProt
- P60513
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conotoxin evia | protein | 32 | 0% helix, 22% strand | P60513 |
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, 1 modified (disulfide, hydroxylation).
Compared structures
- 1G1P · NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts… · the same entry in another collection · chain A against A, TM-score 1.00
- P60513 · AlphaFold monomer V2.0 prediction for delta-conotoxin evia (P60513) · a predicted model of the same protein · chain A against A, TM-score 0.60
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 P60513
- Elsewhere: RCSB PDB 1G1P · PDBe 1G1P · UniProt P60513
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