Research workbench
NMR solution structure of the glucagon antagonist [DESHIS1, DESPHE6, GLU9]GLUCAGON amide in the presence of perdeuterated dodecylphosphocholine micelles
Analyse NMR solution structure of the glucagon antagonist [DESHIS1, DESPHE6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NAU
- Type
- protein
- Length
- 27 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucagon
- UniProt
- P01275
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucagon | protein | 27 | 63% helix, 0% strand | P01275 |
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.
Compared structures
- 1NAU · NMR Solution Structure of the Glucagon Antagonist [desHis1, desPhe6, Glu9]Glucagon Amide… · the same entry in another collection · chain A against A, TM-score 1.00
- P01275 · AlphaFold monomer V2.0 prediction for pro-glucagon (P01275) · a predicted model of the same protein · chain A against A, TM-score 0.53
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 P01275
- Elsewhere: RCSB PDB 1NAU · PDBe 1NAU · UniProt P01275
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