› 6ko5

X-ray diffraction
3.3Å resolution

Complex structure of Ghrelin receptor with Fab

Released:
DOI: 10.2210/pdb6ko5/pdb
PDB entry 6ko5 coloured by chain, front view.
PDB entry 6ko5 coloured by chain, side view.
PDB entry 6ko5 coloured by chain, top view.
Source organisms:
Primary publication:
Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode.
Shiimura Y, Horita S, Hamamoto A, Asada H, Hirata K, Tanaka M, Mori K, Uemura T, Kobayashi T, Iwata S, Kojima M
Nat Commun 11 4160 (2020)
PMID: 32814772

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209566 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Growth hormone secretagogue receptor type 1; Soluble cytochrome b562 Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 47.89 KDa
Source organisms: Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P0ABE7 (Residues: 23-128; Coverage: 100%)
  • Canonical: Q92847 (Residues: 29-346; Coverage: 87%)
Gene names: GHSR, cybC
Sequence domains:
Fab7881 Heavy Chain Chain: H
Molecule details ›
Chain: H
Length: 218 amino acids
Theoretical weight: 23.33 KDa
Source organism: Mus musculus
Fab7881 Light Chain Chain: L
Molecule details ›
Chain: L
Length: 219 amino acids
Theoretical weight: 24.28 KDa
Source organism: Mus musculus

Ligands and Environments

1 bound ligand:
Ligand 8QX 1 x 8QX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: C2
Unit cell:
a: 253.76Å b: 44.75Å c: 94.4Å
α: 90° β: 97.26° γ: 90°
R-values:
R R work R free
0.213 0.21 0.258
Expression system: Spodoptera frugiperda

Quick links

Citations

7 review citations

Relationship between Orexigenic Peptide Ghrelin Signal, Gender Difference and Disease.
Yamada C. (2021)
6 more

16 mentions without citation

Allosteric communication regulates ligand-specific GPCR activity.
Ma et al. (2021)
15 more