XFEL crystal structure of human melatonin receptor MT1 in complex with ramelteon. Determined by X-ray diffraction at 2.8 Å resolution. Released 24 Apr 2019.
Explore 6ME2 in 3D Show helices and sheets RCSB PDB PDBe
6ME2 contains 29 α-helices and 10 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 | 24-54 | 31 | |
| α-helix | 61-63 | 3 | |
| α-helix | 64-78 | 15 | |
| α-helix | 80-90 | 11 | |
| α-helix | 96-134 | 39 | |
| α-helix | 138-139 | 2 | |
| α-helix | 144-159 | 16 | |
| α-helix | 161-165 | 5 | |
| β-strand | 168-171 | 4 | 1 |
| β-strand | 176-179 | 4 | 1 |
| α-helix | 185-192 | 8 | |
| α-helix | 193-197 | 5 | |
| α-helix | 198-1001 | 22 | |
| α-helix | 1009-1011 | 3 | |
| α-helix | 1016-1026 | 11 | |
| β-strand | 1033-1038 | 6 | 2 |
| β-strand | 1041 | 1 | 3 |
| α-helix | 1048-1059 | 12 | |
| α-helix | 1062-1066 | 5 | |
| β-strand | 1067-1072 | 6 | 2 |
| β-strand | 1075 | 1 | 3 |
| α-helix | 1077-1089 | 13 | |
| β-strand | 1093-1096 | 4 | 2 |
| α-helix | 1099-1101 | 3 | |
| α-helix | 1102-1109 | 8 | |
| β-strand | 1114-1117 | 4 | 2 |
| α-helix | 1126-1133 | 8 | |
| α-helix | 1136 | 1 | |
| β-strand | 1137-1141 | 5 | 2 |
| α-helix | 1146-1149 | 4 | |
| β-strand | 1156-1158 | 3 | 2 |
| α-helix | 1163-1174 | 12 | |
| α-helix | 1178-228 | 20 | |
| α-helix | 235-263 | 29 | |
| α-helix | 265-271 | 7 | |
| α-helix | 274-286 | 13 | |
| α-helix | 287-289 | 3 | |
| α-helix | 290-298 | 9 | |
| α-helix | 300-312 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| chimera protein of Melatonin receptor type 1A and GlgA glycogen synthase | A | protein | 503 | Homo sapiens, Pyrococcus abyssi GE5 | P48039 (AlphaFold model), Q9V2J8 (AlphaFold model) |
>6ME2_1 chimera protein of Melatonin receptor type 1A and GlgA glycogen synthase (chains A) GTSQPVLRGDGARPSWLASALACVLIFTIVVDILGNLLVILSVYRNKKLRNAGNIFVVSL AVANLVVAIYPYPLVLMSIFNNGWNFGYLHCQVSAFLMGLSVIGSIWNITGIAIDRYLYI CHSLKYDKLYSSKNSLCYVLLIWLLTLAAVLPNLRAGTLQYDPRIYSCTFAQSVSSAYTI AVVVFHFLVPMIIVIFCYLRIWILVLQVRGIDCSFWNESYLTGSRDERKKSLLSKFGMDE GVTFMFIGRFDRGQKGVDVLLKAIEILSSKKEFQEMRFIIIGKGDPELEGWARSLEEKHG NVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIIT NETGILVKAGDPGELANAILKALELSRSDLSKFRENCKKRAMSFSKLKPQDFRNFVTMFV VFVLFAICFAPLNFIGLAVASDPASMVPRIPEWLFVASYYMAYFNSCLNPIIYGLLDQNF RKEYRRIIVSLCTARVFFVDSSN
| ID | Name | Formula | Copies |
|---|---|---|---|
| OLA | Oleic acid | C18 H34 O2 | 2 |
| JEV | N-{2-[(8S)-1,6,7,8-tetrahydro-2H-indeno[5,4-b]furan-8-yl]ethyl}propanamide | C16 H21 N O2 | 1 |
Water and common crystallization additives (PEG) are not listed.
Structural basis of ligand recognition at the human MT1melatonin receptor. Stauch, B., Johansson, L.C., McCorvy, J.D. et al. Nature (2019) 569:284-288. DOI 10.1038/s41586-019-1141-3 · PubMed
Other PDB entries of the same protein (UniProt P48039 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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