Research workbench
NMR solution structure of omega-conotoxin [K10]GVIA, a cyclic cysteine knot peptide
Analyse NMR solution structure of omega-conotoxin [K10]GVIA, a cyclic cysteine knot… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TR6
- Type
- protein
- Length
- 27 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Omega-conotoxin gvia
- UniProt
- P01522
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Omega-conotoxin gvia | protein | 27 | 0% helix, 22% strand | P01522 |
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, 2 modified (disulfide, hydroxylation).
Compared structures
- 1TR6 · NMR solution structure of omega-conotoxin [K10]GVIA, a cyclic cysteine knot peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P01522 · AlphaFold monomer V2.0 prediction for omega-conotoxin gvia (P01522) · a predicted model of the same protein · chain A against A, TM-score 0.61
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 P01522
- Elsewhere: RCSB PDB 1TR6 · PDBe 1TR6 · UniProt P01522
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