Monitoring the structural Consequences of Phe12-->D-Phe12 and Leu15-->Aib15 substitution in h/r Corticotropin Releasing Hormone: Implications for Design of CRH antagonists. Determined by solution NMR. Released 31 Oct 2001.
Explore 1GOE in 3D Show helices and sheets RCSB PDB PDBe
1GOE contains 2 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 | 6-18 | 13 | |
| α-helix | 20-40 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Corticotropin releasing hormone | A | protein | 42 | HOMO SAPIENS | P06850 (AlphaFold model) |
>1GOE_1 CORTICOTROPIN RELEASING HORMONE (chains A) SEEPPISLDLTFHLAREVLEMARAEQLAQQAHSNRKLMEIIX
Monitoring the Structural Consequences of Phe12-->D-Phe and Leu15-->Aib Substitution in Human/Rat Corticotropin Releasing Hormone. Spyroulias, G.A., Papazacharias, S., Pairas, G. et al. Eur J Biochem (2002) 269:6009. DOI 10.1046/J.1432-1033.2002.03278.X · PubMed
Other PDB entries of the same protein (UniProt P06850 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1GOE directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.