Room Temperature Drosophila Cryptochrome. Determined by X-ray diffraction at 3.5 Å resolution. Released 24 Aug 2022.
Explore 7UD0 in 3D Show helices and sheets RCSB PDB PDBe
7UD0 contains 71 α-helices and 24 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 | 6-11 | 6 | 1 |
| α-helix | 21-26 | 6 | |
| α-helix | 30-32 | 3 | |
| β-strand | 35-42 | 8 | 1 |
| α-helix | 54-75 | 22 | |
| β-strand | 82-85 | 4 | 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 | 143-149 | 7 | |
| α-helix | 158-168 | 11 | |
| α-helix | 171-178 | 8 | |
| β-strand | 185 | 1 | 1 |
| α-helix | 190-195 | 6 | |
| α-helix | 202-204 | 3 | |
| α-helix | 205-208 | 4 | |
| α-helix | 227-247 | 21 | |
| α-helix | 267-271 | 5 | |
| α-helix | 277-287 | 11 | |
| β-strand | 296-297 | 2 | 2 |
| β-strand | 300-301 | 2 | 2 |
| α-helix | 303-305 | 3 | |
| α-helix | 306-321 | 16 | |
| α-helix | 342 | 1 | |
| β-strand | 343 | 1 | 3 |
| α-helix | 344-345 | 2 | |
| α-helix | 347-354 | 8 | |
| α-helix | 361-372 | 12 | |
| α-helix | 378-388 | 11 | |
| β-strand | 395 | 1 | 3 |
| α-helix | 397-407 | 11 | |
| α-helix | 413-424 | 12 | |
| α-helix | 430-433 | 4 | |
| α-helix | 435-438 | 4 | |
| α-helix | 440-447 | 8 | |
| α-helix | 452-457 | 6 | |
| α-helix | 459-461 | 3 | |
| α-helix | 466-469 | 4 | |
| α-helix | 472-474 | 3 | |
| α-helix | 477-482 | 6 | |
| β-strand | 487 | 1 | 4 |
| β-strand | 491 | 1 | 4 |
| α-helix | 492-494 | 3 | |
| α-helix | 498-516 | 19 | |
| α-helix | 519-520 | 2 | |
| α-helix | 528-534 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-11 | 6 | 5 |
| α-helix | 21-26 | 6 | |
| α-helix | 30-32 | 3 | |
| β-strand | 35-42 | 8 | 5 |
| α-helix | 54-75 | 22 | |
| β-strand | 82-85 | 4 | 5 |
| α-helix | 88-98 | 11 | |
| β-strand | 101-107 | 7 | 5 |
| α-helix | 112-114 | 3 | |
| α-helix | 115-127 | 13 | |
| β-strand | 131-135 | 5 | 5 |
| α-helix | 143-149 | 7 | |
| α-helix | 158-168 | 11 | |
| α-helix | 171-178 | 8 | |
| β-strand | 185 | 1 | 5 |
| α-helix | 190-195 | 6 | |
| α-helix | 202-204 | 3 | |
| α-helix | 205-208 | 4 | |
| α-helix | 227-247 | 21 | |
| α-helix | 267-272 | 6 | |
| α-helix | 277-287 | 11 | |
| β-strand | 296-297 | 2 | 6 |
| β-strand | 300-301 | 2 | 6 |
| α-helix | 303-305 | 3 | |
| α-helix | 306-321 | 16 | |
| α-helix | 342 | 1 | |
| β-strand | 343 | 1 | 7 |
| α-helix | 344-345 | 2 | |
| α-helix | 347-354 | 8 | |
| α-helix | 361-372 | 12 | |
| α-helix | 378-388 | 11 | |
| β-strand | 395 | 1 | 7 |
| α-helix | 397-407 | 11 | |
| α-helix | 413-424 | 12 | |
| α-helix | 430-433 | 4 | |
| α-helix | 435-438 | 4 | |
| α-helix | 440-447 | 8 | |
| α-helix | 452-457 | 6 | |
| α-helix | 459-461 | 3 | |
| α-helix | 466-469 | 4 | |
| α-helix | 472-474 | 3 | |
| α-helix | 477-482 | 6 | |
| β-strand | 487 | 1 | 8 |
| β-strand | 491 | 1 | 8 |
| α-helix | 498-516 | 19 | |
| α-helix | 519-520 | 2 | |
| α-helix | 528-534 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cryptochrome-1 | A, B | protein | 539 | Drosophila melanogaster | O77059 (AlphaFold model) |
>7UD0_1 Cryptochrome-1 (chains A, B) MATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFL LDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDES IRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARL EDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKV EQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGV QMTGGAHITGQLIWREYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGF PLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNW MWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQ EQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLAD
| ID | Name | Formula | Copies |
|---|---|---|---|
| FAD | Flavin-adenine dinucleotide | C27 H33 N9 O15 P2 | 2 |
Room-temperature serial synchrotron crystallography of Drosophila cryptochrome. Schneps, C.M., Ganguly, A., Crane, B.R. Acta Crystallogr D Struct Biol (2022) 78:975-985. DOI 10.1107/S2059798322007008 · PubMed
Other PDB entries of the same protein (UniProt O77059 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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