Crystal structure of human alpha2C adrenergic G protein-coupled receptor. Determined by X-ray diffraction at 2.8 Å resolution. Released 4 Dec 2019.
Explore 6KUW in 3D Show helices and sheets RCSB PDB PDBe
6KUW contains 56 α-helices and 16 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 | 42-44 | 3 | |
| α-helix | 48-78 | 31 | |
| α-helix | 80-82 | 3 | |
| α-helix | 85-87 | 3 | |
| α-helix | 88-103 | 16 | |
| α-helix | 105-114 | 10 | |
| α-helix | 120-154 | 35 | |
| α-helix | 156-160 | 5 | |
| α-helix | 165-183 | 19 | |
| β-strand | 189 | 1 | 1 |
| β-strand | 204 | 1 | 1 |
| α-helix | 208-215 | 8 | |
| α-helix | 216-220 | 5 | |
| α-helix | 221-239 | 19 | |
| α-helix | 241-1002 | 3 | |
| α-helix | 1016-1027 | 12 | |
| β-strand | 1033-1037 | 5 | 2 |
| α-helix | 1048-1059 | 12 | |
| α-helix | 1062-1064 | 3 | |
| β-strand | 1067-1072 | 6 | 2 |
| α-helix | 1077-1089 | 13 | |
| β-strand | 1093-1096 | 4 | 2 |
| α-helix | 1102-1109 | 8 | |
| β-strand | 1114-1117 | 4 | 2 |
| α-helix | 1126-1134 | 9 | |
| β-strand | 1137-1141 | 5 | 2 |
| α-helix | 1145-1149 | 5 | |
| β-strand | 1156-1158 | 3 | 2 |
| α-helix | 1159 | 1 | |
| α-helix | 1163-1177 | 15 | |
| α-helix | 1182-408 | 52 | |
| α-helix | 409-412 | 4 | |
| α-helix | 413-415 | 3 | |
| α-helix | 416-428 | 13 | |
| α-helix | 429-431 | 3 | |
| α-helix | 433-440 | 8 | |
| α-helix | 442-452 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 48-76 | 29 | |
| α-helix | 85-87 | 3 | |
| α-helix | 88-99 | 12 | |
| α-helix | 100-104 | 5 | |
| α-helix | 105-114 | 10 | |
| α-helix | 120-154 | 35 | |
| α-helix | 158-161 | 4 | |
| α-helix | 165-183 | 19 | |
| α-helix | 203-205 | 3 | |
| α-helix | 208-215 | 8 | |
| α-helix | 216-220 | 5 | |
| α-helix | 221-237 | 17 | |
| α-helix | 1009-1011 | 3 | |
| α-helix | 1016-1026 | 11 | |
| α-helix | 1029-1031 | 3 | |
| β-strand | 1034-1037 | 4 | 3 |
| β-strand | 1041 | 1 | 4 |
| α-helix | 1048-1058 | 11 | |
| β-strand | 1068-1072 | 5 | 3 |
| β-strand | 1075 | 1 | 4 |
| α-helix | 1077-1089 | 13 | |
| β-strand | 1093-1096 | 4 | 3 |
| α-helix | 1099-1101 | 3 | |
| α-helix | 1102-1109 | 8 | |
| β-strand | 1114-1117 | 4 | 3 |
| α-helix | 1126-1133 | 8 | |
| α-helix | 1136 | 1 | |
| β-strand | 1137-1141 | 5 | 3 |
| α-helix | 1146-1149 | 4 | |
| β-strand | 1156-1158 | 3 | 3 |
| α-helix | 1163-1177 | 15 | |
| α-helix | 1182-408 | 52 | |
| α-helix | 409-411 | 3 | |
| α-helix | 416-440 | 25 | |
| α-helix | 442-452 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-2C adrenergic receptor | A, B | protein | 496 | Homo sapiens | P18825 (AlphaFold model), Q9V2J8 (AlphaFold model) |
>6KUW_1 Alpha-2C adrenergic receptor (chains A, B) GGVANASGASWGPPRGQYSAGAVAGLAAVVGFLIVFTVVGNVLVVIAVLTSRALRAPQNL FLVSLASADILVATLVMPFSLANELMAYWYFGQWWCGVYLALDVLFCTSSAVHLCAISLD RYWSVTQAVEYNLKRTPRRVKATIVAVWLISAVISFPPLVSLYRQPDGAAYPQCGLNDET WYILSSCIGSFFAPCLIMGLVYARIYRVAKLRTGIDCSFWNESYLTGSRDERKKSLLSKF GMDEGVTFMFIGRFDRGQKGVDVLLKAIEILSSKKEFQEMRFIIIGKGDPELEGWARSLE EKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLR DIITNETGILVKAGDPGELANAILKALELSRSDLSKFRENCKKRAMSFSVAQAREKRFTF VLAVVMGVWVLCWFPFFFSYSLYGICREACQVPGPLFKFFFWIGYCNSSLNPVIYTVFNQ DFRRSFKHILFRRRRR
| ID | Name | Formula | Copies |
|---|---|---|---|
| OLA | Oleic acid | C18 H34 O2 | 2 |
| OLC | (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate | C21 H40 O4 | 7 |
| CLR | Cholesterol | C27 H46 O | 2 |
| E33 | (8~{a}~{R},12~{a}~{S},13~{a}~{R})-12-ethylsulfonyl-3-methoxy-5,6,8,8~{a},9,10,1… | C19 H28 N2 O3 S | 2 |
Crystal structure of human alpha2C adrenergic G protein-coupled receptor. Chen, X.Y., Wu, D., Wu, L.J. et al. To be published.
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