MolNFT v1 · #2063 · protein
Effects of glycosylation on the structure and dynamics of eel calcitonin, NMR, 10 structures
1BKU: “Effects of glycosylation on the structure and dynamics of eel calcitonin, NMR, 10 structures”. Solution nmr, 1 ligand (NH2). MolNFT v1 #2063 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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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