Research workbench
Structure of the calcium channel blocker omega conotoxin gvia, NMR, 20 structures
Analyse Structure of the calcium channel blocker omega conotoxin gvia, NMR, 20… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CCO
- 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, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Omega-conotoxin gvia | protein | 27 | 0% helix, 30% 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, 3 modified (disulfide, hydroxylation).
Compared structures
- 2CCO · Structure of the calcium channel blocker omega conotoxin gvia, NMR, 20 structures · 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 0.63
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 2CCO · PDBe 2CCO · UniProt P01522
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