Crystal structure of the CLR:RAMP2 extracellular domain heterodimer with bound adrenomedullin. Determined by X-ray diffraction at 1.76 Å resolution. Released 20 May 2015.
Explore 4RWF in 3D Show helices and sheets RCSB PDB PDBe
4RWF contains 32 α-helices and 38 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-5 | 2 | |
| β-strand | 9-12 | 4 | 1 |
| α-helix | 19-33 | 15 | |
| β-strand | 37-40 | 4 | 1 |
| α-helix | 45-54 | 10 | |
| β-strand | 61-65 | 5 | 1 |
| α-helix | 66-68 | 3 | |
| α-helix | 69-74 | 6 | |
| β-strand | 78 | 1 | 2 |
| α-helix | 79-81 | 3 | |
| α-helix | 85-88 | 4 | |
| β-strand | 91 | 1 | 3 |
| α-helix | 93-98 | 6 | |
| β-strand | 100-101 | 2 | 4 |
| β-strand | 104-105 | 2 | 4 |
| β-strand | 108-113 | 6 | 1 |
| β-strand | 116-120 | 5 | 5 |
| β-strand | 130 | 1 | 6 |
| α-helix | 134-142 | 9 | |
| β-strand | 147-149 | 3 | 5 |
| α-helix | 156-165 | 10 | |
| β-strand | 169 | 1 | 7 |
| β-strand | 173-174 | 2 | 8 |
| β-strand | 177-178 | 2 | 8 |
| β-strand | 184 | 1 | 7 |
| α-helix | 188-202 | 15 | |
| α-helix | 212-220 | 9 | |
| β-strand | 224-229 | 6 | 5 |
| α-helix | 231-233 | 3 | |
| α-helix | 234-240 | 7 | |
| β-strand | 244-247 | 4 | 5 |
| α-helix | 248-250 | 3 | |
| β-strand | 251 | 1 | 6 |
| β-strand | 252 | 1 | 9 |
| β-strand | 255 | 1 | 9 |
| α-helix | 259 | 1 | |
| β-strand | 260-261 | 2 | 10 |
| β-strand | 262-268 | 7 | 1 |
| β-strand | 269 | 1 | 2 |
| α-helix | 275-280 | 6 | |
| α-helix | 281-286 | 6 | |
| α-helix | 289-298 | 10 | |
| β-strand | 303-304 | 2 | 1 |
| β-strand | 306 | 1 | 3 |
| α-helix | 307-313 | 7 | |
| α-helix | 317-328 | 12 | |
| β-strand | 330-331 | 2 | 10 |
| α-helix | 332-333 | 2 | |
| α-helix | 338-353 | 16 | |
| α-helix | 359-374 | 16 | |
| α-helix | 1061-1076 | 16 | |
| α-helix | 1077-1082 | 6 | |
| α-helix | 1086-1106 | 21 | |
| α-helix | 1114-1126 | 13 | |
| α-helix | 2036-2054 | 19 | |
| β-strand | 2064-2065 | 2 | 11 |
| α-helix | 2066-2067 | 2 | |
| β-strand | 2068-2069 | 2 | 12 |
| β-strand | 2074-2075 | 2 | 12 |
| β-strand | 2078-2079 | 2 | 11 |
| β-strand | 2082-2087 | 6 | 13 |
| α-helix | 2088-2089 | 2 | |
| β-strand | 2092 | 1 | 14 |
| β-strand | 2100-2105 | 6 | 13 |
| β-strand | 2111 | 1 | 13 |
| β-strand | 2113-2114 | 2 | 15 |
| β-strand | 2119-2120 | 2 | 15 |
| β-strand | 2123 | 1 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 39 | 1 | 14 |
| α-helix | 44-47 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related… | A | protein | 591 | Escherichia coli, Homo sapiens | O60895 (AlphaFold model), P0AEX9 (AlphaFold model), Q16602 (AlphaFold model) |
| Adrenomedullin | B | protein | 29 | Homo sapiens | P35318 (AlphaFold model) |
>4RWF_1 Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein (chains A) MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD EALKDAQTNAAAEFGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCL EHFAERFDLGFPNPLAERIIFETHQIHFANCSLVQPTFSDGSAGSAGSAEDSIQLGVTRN KIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSE KVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLHHHHHH
>4RWF_2 Adrenomedullin (chains B) KLAHQIYQFTDKDKDNVAPRSKISPQGYX
Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor. Booe, J.M., Walker, C.S., Barwell, J. et al. Mol Cell (2015) 58:1-13. DOI 10.1016/j.molcel.2015.04.018 · PubMed
Other PDB entries of the same protein (UniProt O60895 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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