Research workbench
[PRO7,13] aa-conotoxin piva, NMR, 12 structures
Analyse [PRO7,13] aa-conotoxin piva, NMR, 12 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P1P
- Type
- protein
- Length
- 25 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aa-conotoxin piva
- UniProt
- P55963
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 12% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aa-conotoxin piva | protein | 25 | 12% helix, 0% strand | P55963 |
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
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 P55963
- Elsewhere: RCSB PDB 1P1P · PDBe 1P1P · UniProt P55963
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