Research workbench
Effects of glycosylation on the structure and dynamics of eel calcitonin, NMR, 10 structures
Analyse Effects of glycosylation on the structure and dynamics of eel calcitonin, NMR… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BKU
- Type
- protein
- Length
- 32 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcitonin
- UniProt
- P01262
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 47% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcitonin | protein | 32 | 47% helix, 0% strand | P01262 |
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: 1 disulfide (disulfide).
Compared structures
- 1BKU · Effects of glycosylation on the structure and dynamics of eel calcitonin, NMR, 10… · the same entry in another collection · chain A against A, TM-score 1.00
- P01262 · AlphaFold monomer V2.0 prediction for calcitonin (P01262) · a predicted model of the same protein · chain A against A, TM-score 0.55
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 1BKU · PDBe 1BKU · UniProt P01262
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