Research workbench
Glycosylated eel calcitonin
Analyse Glycosylated eel calcitonin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BZB
- Type
- protein
- Length
- 32 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (calcitonin)
- UniProt
- P01262
- Ligands
- MAN, NAG, NH2
Structure
solution nmr · 1 distinct chain · 50% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (calcitonin) | protein | 32 | 50% helix, 0% strand | P01262 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 6 copies
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- 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: 1 disulfide, 1 glycan (disulfide, N-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 P01262
- Elsewhere: RCSB PDB 1BZB · PDBe 1BZB · UniProt P01262
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