Research workbench
NMR structure of the glycosylated conotoxin cctx from conus consors
Analyse NMR structure of the glycosylated conotoxin cctx from conus consors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B1Q
- Type
- protein
- Length
- 30 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conotoxin cctx
- UniProt
- P58928
- Ligands
- GXL, A2G, GAL, NDG
Structure
solution nmr · 1 distinct chain · 13% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Conotoxin cctx | protein | 30 | 13% helix, 0% strand | P58928 |
Ligands and binding sites
- GXL · alpha-L-galactopyranose · ligand · 2 copies · chains P
- A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · sugar · chains P
- GAL · beta-D-galactopyranose · sugar · chains P
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 3 modified, 1 glycan (disulfide, hydroxylation, O-glycosylation).
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 P58928
- Elsewhere: RCSB PDB 4B1Q · PDBe 4B1Q · UniProt P58928
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