The Cryo-EM structure of Drosophila Cryptochrome in complex with Timeless. Determined by electron microscopy at 3.3 Å resolution. Released 15 Feb 2023.
Explore 8DD7 in 3D Show helices and sheets RCSB PDB PDBe
8DD7 contains 80 α-helices and 15 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 |
|---|---|---|---|
| β-strand | 6-10 | 5 | 1 |
| β-strand | 18 | 1 | 2 |
| α-helix | 21-27 | 7 | |
| β-strand | 35-41 | 7 | 1 |
| α-helix | 54-74 | 21 | |
| β-strand | 82-84 | 3 | 1 |
| α-helix | 88-98 | 11 | |
| β-strand | 101-107 | 7 | 1 |
| α-helix | 112-114 | 3 | |
| α-helix | 115-127 | 13 | |
| β-strand | 131-135 | 5 | 1 |
| α-helix | 143-150 | 8 | |
| α-helix | 158-168 | 11 | |
| α-helix | 170-174 | 5 | |
| β-strand | 177 | 1 | 2 |
| α-helix | 180-182 | 3 | |
| α-helix | 187-189 | 3 | |
| α-helix | 190-195 | 6 | |
| α-helix | 205-208 | 4 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-218 | 5 | |
| α-helix | 227-245 | 19 | |
| α-helix | 252-255 | 4 | |
| α-helix | 268-272 | 5 | |
| α-helix | 277-293 | 17 | |
| α-helix | 310-320 | 11 | |
| α-helix | 342-344 | 3 | |
| α-helix | 347-354 | 8 | |
| α-helix | 361-372 | 12 | |
| α-helix | 378-389 | 12 | |
| α-helix | 397-407 | 11 | |
| α-helix | 413-423 | 11 | |
| α-helix | 440-447 | 8 | |
| α-helix | 452-457 | 6 | |
| α-helix | 472-474 | 3 | |
| α-helix | 477-483 | 7 | |
| β-strand | 487 | 1 | 3 |
| β-strand | 491 | 1 | 3 |
| α-helix | 492-494 | 3 | |
| α-helix | 498-516 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| α-helix | 7-17 | 11 | |
| β-strand | 18-21 | 4 | 4 |
| β-strand | 24-27 | 4 | 4 |
| α-helix | 31-43 | 13 | |
| α-helix | 51-59 | 9 | |
| α-helix | 61 | 1 | |
| α-helix | 62-66 | 5 | |
| α-helix | 67-72 | 6 | |
| α-helix | 76-89 | 14 | |
| α-helix | 93-95 | 3 | |
| α-helix | 99-102 | 4 | |
| α-helix | 106-126 | 21 | |
| α-helix | 129-143 | 15 | |
| α-helix | 149-150 | 2 | |
| α-helix | 151-169 | 19 | |
| α-helix | 172 | 1 | |
| α-helix | 173-177 | 5 | |
| α-helix | 185-201 | 17 | |
| α-helix | 204-213 | 10 | |
| α-helix | 217-219 | 3 | |
| α-helix | 221-231 | 11 | |
| α-helix | 237-247 | 11 | |
| α-helix | 546-570 | 25 | |
| α-helix | 578-591 | 14 | |
| α-helix | 592-596 | 5 | |
| α-helix | 597-608 | 12 | |
| α-helix | 618-634 | 17 | |
| α-helix | 639-641 | 3 | |
| α-helix | 648-668 | 21 | |
| α-helix | 677-702 | 26 | |
| α-helix | 708-722 | 15 | |
| α-helix | 730-736 | 7 | |
| α-helix | 745-765 | 21 | |
| α-helix | 776-779 | 4 | |
| α-helix | 787-797 | 11 | |
| α-helix | 799-802 | 4 | |
| α-helix | 807-818 | 12 | |
| α-helix | 830-842 | 13 | |
| α-helix | 851-854 | 4 | |
| α-helix | 859-862 | 4 | |
| α-helix | 991-1001 | 11 | |
| α-helix | 1006-1017 | 12 | |
| α-helix | 1020-1027 | 8 | |
| β-strand | 1033 | 1 | 5 |
| β-strand | 1036 | 1 | 5 |
| α-helix | 1040-1046 | 7 | |
| β-strand | 1054 | 1 | 6 |
| α-helix | 1059-1062 | 4 | |
| α-helix | 1063-1066 | 4 | |
| α-helix | 1068-1076 | 9 | |
| β-strand | 1090 | 1 | 6 |
| α-helix | 1091 | 1 | |
| α-helix | 1103-1107 | 5 | |
| α-helix | 1210-1218 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Methylated-DNA--protein-cysteine methyltransferase,Cryptochrome-1 fusion | A | protein | 746 | Homo sapiens, Drosophila melanogaster | E5BBQ0 (AlphaFold model), O77059 (AlphaFold model) |
| Protein timeless,Methylated-DNA--protein-cysteine methyltransferase fusion | B | protein | 1618 | Drosophila melanogaster, Homo sapiens | E5BBQ0 (AlphaFold model), P49021 (AlphaFold model) |
>8DD7_1 Methylated-DNA--protein-cysteine methyltransferase,Cryptochrome-1 fusion (chains A) MEQKLISEEDLGGGEQKLISEEDLGGGEQKLISEEDLGGGMDKDCEMKRTTLDSPLGKLE LSGCEQGLHRIIFLGKGTSAADAVEVPAPAAVLGGPEPLIQATAWLNAYFHQPEAIEEFP VPALHHPVFQQESFTRQVLWKLLKVVKFGEVISESHLAALVGNPAATAAVNTALDGNPVP ILIPCHRVVQGDSDVGPYLGGLAVKEWLLAHEGHRLGKPGLGGGSGMATRGANVIWFRHG LRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAA TDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVE KVSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARLEDATFVELDPEFCR SLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKVEQHAFERGFYLPNQ ALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIW REYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEG WLHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDS SLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQEQYECLIGVHYPER IIDLSMAVKRNMLAMKSLRNSLITPP
>8DD7_2 Protein timeless,Methylated-DNA--protein-cysteine methyltransferase fusion (chains B) MDWLLATPQLYSAFSSLGCLEGDTYVVNPNALAILEEINYKLTYEDQTLRTFRRAIGFGQ NVRSDLIPLLENAKDDAVLESVIRILVNLTVPVECLFSVDVMYRTDVGRHTIFELNKLLY TSKEAFTEARSTKSVVEYMKHILESDPKLSPHKCDQINNCLLLLRNILHIPETHAHCVMP MMQSMPHGISMQNTILWNLFIQSIDKLLLYLMTCPQRAFWGVTMVQLIALIYKDQHVSTL QKLLSLWFEASLSESSEDNESNTSPPKQGSGDSSPMLTSDPTSDSSDNGSNGRGMGGGMR EGTAATLQEVSRKGQEYQNAMARVPADKPDGSEEASDMTGNDSEQPGSPEQSQPAGESMD DGDYEDQRHRQLNEHGEEDEDEDEVEEEEYLQLGPASEPLNLTQQPADKVNNTTNPTSSA PQGCLGNEPFKPPPPLPVRASTSAHAQMQKFNESSYASHVSAVKLGQKSPHAGQLQLTKG KCCPQKRECPSSQSELSDCGYGTQVENQESISTSSNDDDGPQGKPQHQKPPCNTKPRNKP RTIMSPMDKKELRRKKLVKRSKSSLINMKGLVQHTPTDDDISNLLKEFTVDFLLKGYSYL VEELHMQLLSNAKVPIDTSHFFWLVTYFLKFAAQLELDMEHIDTILTYDVLSYLTYEGVS LCEQLELNARQEGSDLKPYLRRMHLVVTAIREFLQAIDTYNKVTHLNEDDKAHLRQLQLQ ISEMSDLRCLFVLLLRRFNPSIHSKQYLQDLVVTNHILLLILDSSAKLGGCQTIRLSEHI TQFATLEVMHYYGILLEDFNNNGEFVNDCIFTMMHHIGGDLGQIGVLFQPIILKTYSRIW EADYELCDDWSDLIEYVIHKFMNTPPKSPLTIPTTSLTEMTKEHNQEHTVCSWSQEEMDT LYWYYVQSKKNNDIVGKIVKLFSNNGNKLKTRISIIQQLLQQDIITLLEYDDLMKFEDAE YQRTLLTTPTSATTESGIEIKECAYGKPSDDVQILLDLIIKENKAQHLLWLQRILIECCF VKLTLRSGLKVPEGDHIMEPVAYHCICKQKSIPVVQWNNEQSTTMLYQPFVLLLHKLGIQ LPADAGSIFARIPDYWTPETMYGLAKKLGPLDKLNLKFDASELEDATASSPSRYHHTGPR NSLSSVSSLDVDLGDTEELALIPEVDAAVEKAHAMASTPSPSEIFAVPKTKHCNSIIRYT PDPTPPVPNWLQLVMRSKCNHRTGPSGDPSDCIGSSSTTVDDEGFGKSISAATSQAASTS MSTVNPTTTLSLNMLNTFMGSHNENSSSSGCGGTVSSLSMVALMSTGAAGGGGNTSGLEM DVDASMKSSFERLEVNGSHFSRANNLDQEYSAMVASVYEKEKELNSDNVSLASDLTRMYV SDEDDRLERTEIRVPHYHLEGGSGMDKDCEMKRTTLDSPLGKLELSGCEQGLHRIIFLGK GTSAADAVEVPAPAAVLGGPEPLMQATAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTR QVLWKLLKVVKFGEVISYSHLAALAGNPAATAAVKTALSGNPVPILIPCHRVVQGDLDVG GYEGGLAVKEWLLAHEGHRLGKPGLGGGGYPYDVPDYARTGGGSGSRLEEELRRRLTE
| ID | Name | Formula | Copies |
|---|---|---|---|
| FAD | Flavin-adenine dinucleotide | C27 H33 N9 O15 P2 | 1 |
Cryptochrome-Timeless structure reveals circadian clock timing mechanisms. Lin, C., Feng, S., DeOliveira, C.C. et al. Nature (2023) 617:194-199. DOI 10.1038/s41586-023-06009-4 · PubMed
Other PDB entries of the same protein (UniProt E5BBQ0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8DD7 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.