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Exendin-4 variant with dual glp-1 / glucagon receptor activity

Analyse Exendin-4 variant with dual glp-1 / glucagon receptor activity in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NIQ
Type
protein
Length
39 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Exendin-4
Ligands
D6M, NH2

Structure

solution nmr · 1 distinct chain · 69% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AExendin-4protein3969% helix, 0% strand—

Ligands and binding sites

  • D6M · N-hexadecanoyl-L-glutamic acid · ligand · 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 covalent, 1 d-amino (covalent ligand, D-amino acid).

Compared structures

  • 5NIQ · exendin-4 variant with dual GLP-1 / glucagon receptor activity · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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