exendin-4 variant with dual GLP-1 / glucagon receptor activity. Determined by solution NMR. Released 28 Feb 2018.
Explore 5NIQ in 3D Show helices and sheets RCSB PDB PDBe
5NIQ contains 3 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-28 | 23 | |
| α-helix | 30-33 | 4 | |
| α-helix | 36-37 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Exendin-4 | A | protein | 40 | Heloderma suspectum | P26349 (AlphaFold model) |
>5NIQ_1 Exendin-4 (chains A) HSQGTFTSDLSKQKDSRRAQDFIEWLKNGGPSSGAPPPSX
| ID | Name | Formula | Copies |
|---|---|---|---|
| D6M | N-hexadecanoyl-L-glutamic acid | C21 H39 N O5 | 1 |
Design of Novel Exendin-Based Dual Glucagon-like Peptide 1 (GLP-1)/Glucagon Receptor Agonists. Evers, A., Haack, T., Lorenz, M. et al. J Med Chem (2017) 60:4293-4303. DOI 10.1021/acs.jmedchem.7b00174 · PubMed
Other PDB entries of the same protein (UniProt P26349 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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