Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1). Determined by X-ray diffraction at 2.76 Å resolution. Released 30 Sept 2008.
Explore 3EHS in 3D Show helices and sheets RCSB PDB PDBe
3EHS contains 30 α-helices and 31 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 | -347--346 | 2 | |
| β-strand | -345 | 1 | 1 |
| β-strand | -343--339 | 5 | 1 |
| α-helix | -332--318 | 15 | |
| β-strand | -315--311 | 5 | 1 |
| α-helix | -306--298 | 9 | |
| β-strand | -290--286 | 5 | 1 |
| α-helix | -285--283 | 3 | |
| α-helix | -282--276 | 7 | |
| β-strand | -273 | 1 | 2 |
| α-helix | -272--270 | 3 | |
| α-helix | -266--262 | 5 | |
| β-strand | -260 | 1 | 3 |
| α-helix | -258--253 | 6 | |
| β-strand | -251--250 | 2 | 4 |
| β-strand | -247--246 | 2 | 4 |
| β-strand | -243--238 | 6 | 1 |
| β-strand | -235--231 | 5 | 5 |
| β-strand | -221 | 1 | 6 |
| α-helix | -220--218 | 3 | |
| α-helix | -217--210 | 8 | |
| β-strand | -204--202 | 3 | 5 |
| α-helix | -195--186 | 10 | |
| β-strand | -182--178 | 5 | 7 |
| β-strand | -173--167 | 7 | 7 |
| α-helix | -163--149 | 15 | |
| α-helix | -139--130 | 10 | |
| β-strand | -127--122 | 6 | 5 |
| α-helix | -117--111 | 7 | |
| β-strand | -107--104 | 4 | 5 |
| α-helix | -103--101 | 3 | |
| β-strand | -100--99 | 2 | 6 |
| β-strand | -96--95 | 2 | 6 |
| α-helix | -94 | 1 | |
| β-strand | -91--90 | 2 | 8 |
| β-strand | -89--83 | 7 | 1 |
| β-strand | -82 | 1 | 2 |
| α-helix | -76--70 | 7 | |
| α-helix | -69--65 | 5 | |
| α-helix | -62--53 | 10 | |
| β-strand | -48--47 | 2 | 1 |
| β-strand | -45 | 1 | 3 |
| α-helix | -44--38 | 7 | |
| α-helix | -34--23 | 12 | |
| β-strand | -21--20 | 2 | 8 |
| α-helix | -19--18 | 2 | |
| α-helix | -13-2 | 16 | |
| α-helix | 8-19 | 12 | |
| α-helix | 25-35 | 11 | |
| α-helix | 38-40 | 3 | |
| β-strand | 43-44 | 2 | 9 |
| α-helix | 45-46 | 2 | |
| β-strand | 47-48 | 2 | 10 |
| β-strand | 54-55 | 2 | 10 |
| β-strand | 58-59 | 2 | 9 |
| β-strand | 62-72 | 11 | 11 |
| β-strand | 75-87 | 13 | 11 |
| α-helix | 88 | 1 | |
| α-helix | 92 | 1 | |
| β-strand | 93-98 | 6 | 11 |
| α-helix | 103-107 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| fusion protein of CRFR1 extracellular domain and MBP | A | protein | 476 | Escherichia coli, Homo sapiens | P0AEX9 (AlphaFold model), P34998 (AlphaFold model) |
>3EHS_1 fusion protein of CRFR1 extracellular domain and MBP (chains A) MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD EALKDAQTNAAAEFSLQDQHCESLSLASNISGLQCNASVDLIGTCWPRSPAGQLVVRPCP AFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAHHHHHH
Molecular Recognition of Corticotropin-releasing Factor by Its G-protein-coupled Receptor CRFR1. Pioszak, A.A., Parker, N.R., Suino-Powell, K. et al. J Biol Chem (2008) 283:32900-32912. DOI 10.1074/jbc.M805749200 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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