8GJI: GCG binder

De novo design of high-affinity protein binders to bioactive helical peptides. Determined by X-ray diffraction at 1.81 Å resolution. Released 10 Jan 2024.

Method: X-ray diffraction
Resolution: 1.81 Å
Organism: synthetic construct
Chains: 2
Atoms: 1,603
Mol. weight: 24.06 kDa
Released: 10 Jan 2024

Explore 8GJI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8GJI contains 7 α-helices and 0 β-strands across 2 chains. 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.

Chain A: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	4-35	32
α-helix	39-73	35
α-helix	77-108	32
α-helix	111-141	31
α-helix	145-168	24

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	183-185	3
α-helix	187-198	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GCG binder	A	protein	174	synthetic construct
Glucagon	B	protein	29	synthetic construct	P01273 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8GJI_1 GCG binder (chains A)
MSGSMEKLAEIMQEIIEAYQEVKDAFFKFIKAVHEGAPEEELKKYLEKMKEALEKMKELL
ERLEKEAKKVIEENKDKKLELKVLLMLRLAYLLLKVSIELTKIAAEKLGDKELVEELEKE
SKEVEKKIKELEERIKKLLEEVDDEELKEAYKEVEEMEKEAEKFLEKMRKVGSG

Sequence of entity 2 (B), FASTA

>8GJI_2 Glucagon (chains B)
HSQGTFTSDYSKYLDSRRAQDFVQWLMNT

Primary citation

De novo design of high-affinity binders of bioactive helical peptides. Vazquez Torres, S., Leung, P.J.Y., Venkatesh, P. et al. Nature (2024) 626:435-442. DOI 10.1038/s41586-023-06953-1 · PubMed

Other PDB entries of the same protein (UniProt P01273 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9MXU 2.5 Å, cryo-EM structure of GLP-1R-Gs complex with glucagon
9MZG 3.0 Å, Cryo-EM structure of GCGR-Gs complex with glucagon

Browse structure collections

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