Alternative crystal structure of mouse Cryptochrome 2 in complex with TH301 compound. Determined by X-ray diffraction at 2.6 Å resolution. Released 23 Jun 2021.
Explore 7EJ9 in 3D Show helices and sheets RCSB PDB PDBe
7EJ9 contains 68 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 |
|---|---|---|---|
| β-strand | 22-27 | 6 | 1 |
| α-helix | 37-43 | 7 | |
| β-strand | 48-55 | 8 | 1 |
| α-helix | 59-61 | 3 | |
| α-helix | 67-85 | 19 | |
| β-strand | 91-95 | 5 | 1 |
| α-helix | 98-108 | 11 | |
| β-strand | 113-117 | 5 | 1 |
| α-helix | 122-138 | 17 | |
| β-strand | 141-145 | 5 | 1 |
| α-helix | 153-159 | 7 | |
| α-helix | 168-176 | 9 | |
| α-helix | 179-189 | 11 | |
| α-helix | 190-195 | 6 | |
| α-helix | 197-199 | 3 | |
| α-helix | 204-208 | 5 | |
| α-helix | 210-212 | 3 | |
| α-helix | 223-226 | 4 | |
| α-helix | 232-242 | 11 | |
| α-helix | 245-248 | 4 | |
| α-helix | 249-253 | 5 | |
| α-helix | 259-262 | 4 | |
| α-helix | 264-265 | 2 | |
| α-helix | 270-275 | 6 | |
| α-helix | 280-294 | 15 | |
| α-helix | 302-305 | 4 | |
| α-helix | 306-318 | 13 | |
| α-helix | 334-335 | 2 | |
| β-strand | 339 | 1 | 2 |
| α-helix | 342-349 | 8 | |
| α-helix | 356-368 | 13 | |
| α-helix | 373-383 | 11 | |
| β-strand | 390 | 1 | 2 |
| α-helix | 392-402 | 11 | |
| α-helix | 408-419 | 12 | |
| α-helix | 430-432 | 3 | |
| α-helix | 435-440 | 6 | |
| α-helix | 445-450 | 6 | |
| α-helix | 452-454 | 3 | |
| α-helix | 459-462 | 4 | |
| α-helix | 465-467 | 3 | |
| α-helix | 470-475 | 6 | |
| β-strand | 480 | 1 | 3 |
| β-strand | 484 | 1 | 3 |
| α-helix | 485-487 | 3 | |
| α-helix | 491-505 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-27 | 6 | 4 |
| α-helix | 37-43 | 7 | |
| β-strand | 48-55 | 8 | 4 |
| α-helix | 59-61 | 3 | |
| α-helix | 63-64 | 2 | |
| α-helix | 67-85 | 19 | |
| β-strand | 91-95 | 5 | 4 |
| α-helix | 98-108 | 11 | |
| β-strand | 113-117 | 5 | 4 |
| α-helix | 122-137 | 16 | |
| β-strand | 141-145 | 5 | 4 |
| α-helix | 153-159 | 7 | |
| α-helix | 168-176 | 9 | |
| α-helix | 179-189 | 11 | |
| α-helix | 190-195 | 6 | |
| α-helix | 197-199 | 3 | |
| α-helix | 204-208 | 5 | |
| α-helix | 232-247 | 16 | |
| α-helix | 264-265 | 2 | |
| α-helix | 270-275 | 6 | |
| α-helix | 280-294 | 15 | |
| α-helix | 302-305 | 4 | |
| α-helix | 306-318 | 13 | |
| α-helix | 334-335 | 2 | |
| α-helix | 342-350 | 9 | |
| α-helix | 356-368 | 13 | |
| α-helix | 373-383 | 11 | |
| α-helix | 392-402 | 11 | |
| α-helix | 408-418 | 11 | |
| α-helix | 435-440 | 6 | |
| α-helix | 445-450 | 6 | |
| α-helix | 452-456 | 5 | |
| α-helix | 465-467 | 3 | |
| α-helix | 470-475 | 6 | |
| β-strand | 480 | 1 | 5 |
| β-strand | 484 | 1 | 5 |
| α-helix | 485-487 | 3 | |
| α-helix | 491-505 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cryptochrome-2 | A, B | protein | 514 | Mus musculus | Q9R194 (AlphaFold model) |
>7EJ9_1 Cryptochrome-2 (chains A, B) GTMAAAAVVAATVPAQSMGADGASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPW FAASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEY DSEPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQALISRM ELPKKPAVAVSSQQMESCRAEIQENHDDTYGVPSLEELGFPTEGLGPAVWQGGETEALAR LDKHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNS TPPLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWI DAIMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWL SCSAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKGFPSRYIYEPWNAPESVQKAAKC IIGVDYPRPIVNHAETSRLNIERMKQIYQQLSRY
| ID | Name | Formula | Copies |
|---|---|---|---|
| DYX | 1-(4-chlorophenyl)-N-[2-(4-methoxyphenyl)-5,5-bis(oxidanylidene)-4,6-dihydrothi… | C24 H24 Cl N3 O4 S | 2 |
Structural differences in the FAD-binding pockets and lid loops of mammalian CRY1 and CRY2 for isoform-selective regulation. Miller, S., Srivastava, A., Nagai, Y. et al. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2026191118 · PubMed
Other PDB entries of the same protein (UniProt Q9R194 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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