High resolution structure of mouse Cryptochrome 1. Determined by X-ray diffraction at 1.84 Å resolution. Released 8 Feb 2017.
Explore 5T5X in 3D Show helices and sheets RCSB PDB PDBe
5T5X contains 30 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 |
|---|---|---|---|
| β-strand | 4-9 | 6 | 1 |
| α-helix | 19-25 | 7 | |
| β-strand | 30-36 | 7 | 1 |
| α-helix | 49-67 | 19 | |
| β-strand | 73-76 | 4 | 1 |
| α-helix | 80-91 | 12 | |
| β-strand | 93-99 | 7 | 1 |
| α-helix | 104-119 | 16 | |
| β-strand | 123-127 | 5 | 1 |
| α-helix | 135-141 | 7 | |
| α-helix | 150-158 | 9 | |
| β-strand | 179 | 1 | 1 |
| α-helix | 186-190 | 5 | |
| α-helix | 191-194 | 4 | |
| α-helix | 214-229 | 16 | |
| α-helix | 241-244 | 4 | |
| α-helix | 246-247 | 2 | |
| α-helix | 252-257 | 6 | |
| α-helix | 262-277 | 16 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-300 | 13 | |
| α-helix | 316-317 | 2 | |
| β-strand | 321 | 1 | 2 |
| α-helix | 324-332 | 9 | |
| α-helix | 338-350 | 13 | |
| α-helix | 355-363 | 9 | |
| α-helix | 364-368 | 5 | |
| β-strand | 372 | 1 | 2 |
| α-helix | 374-384 | 11 | |
| α-helix | 390-400 | 11 | |
| α-helix | 417-422 | 6 | |
| α-helix | 427-432 | 6 | |
| α-helix | 434-436 | 3 | |
| α-helix | 447-449 | 3 | |
| α-helix | 452-457 | 6 | |
| β-strand | 462 | 1 | 3 |
| β-strand | 466 | 1 | 3 |
| α-helix | 467-469 | 3 | |
| α-helix | 473-487 | 15 | |
| α-helix | 489-490 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cryptochrome-1 | A | protein | 491 | Mus musculus | P97784 (AlphaFold model) |
>5T5X_1 Cryptochrome-1 (chains A) MGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQCLE DLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLATEA GVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLVSKMEPLEMPADTITSDVIGKCMT PLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPRMN ANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYTAA TNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHA VACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGFGR RTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASRLN IERMKQIYQQL
Formation of a repressive complex in the mammalian circadian clock is mediated by the secondary pocket of CRY1. Michael, A.K., Fribourgh, J.L., Chelliah, Y. et al. Proc Natl Acad Sci U S A (2017) 114:1560-1565. DOI 10.1073/pnas.1615310114 · PubMed
Other PDB entries of the same protein (UniProt P97784 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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