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Structure-activity relationships of mu-conotoxin giiia: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations
Analyse Structure-activity relationships of mu-conotoxin giiia: structure determination… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TCH
- Type
- protein
- Length
- 22 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mu-conotoxin giiia
- UniProt
- P01523
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mu-conotoxin giiia | protein | 22 | 0% helix, 0% strand | P01523 |
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
- 1TCH · Structure-activity relationships of mu-conotoxin giiia: structure determination of active… · the same entry in another collection · chain A against A, TM-score 1.00
- P01523 · AlphaFold monomer V2.0 prediction for mu-conotoxin giiia (P01523) · a predicted model of the same protein · chain A against A, TM-score 0.35
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 P01523
- Elsewhere: RCSB PDB 1TCH · PDBe 1TCH · UniProt P01523
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