Crystal structure of mouse CRY1 with bound cryoprotectant. Determined by X-ray diffraction at 1.95 Å resolution. Released 23 Jun 2021.
Explore 7D0M in 3D Show helices and sheets RCSB PDB PDBe
7D0M contains 37 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 | 30-37 | 8 | 1 |
| α-helix | 42-44 | 3 | |
| α-helix | 49-68 | 20 | |
| β-strand | 73-77 | 5 | 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 | 150-159 | 10 | |
| α-helix | 161-169 | 9 | |
| α-helix | 172-175 | 4 | |
| β-strand | 179 | 1 | 1 |
| α-helix | 186-190 | 5 | |
| α-helix | 191-194 | 4 | |
| α-helix | 196-198 | 3 | |
| α-helix | 205-208 | 4 | |
| α-helix | 214-231 | 18 | |
| α-helix | 236-239 | 4 | |
| α-helix | 241-244 | 4 | |
| α-helix | 252-257 | 6 | |
| α-helix | 262-277 | 16 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-300 | 13 | |
| α-helix | 320 | 1 | |
| β-strand | 321 | 1 | 2 |
| α-helix | 322 | 1 | |
| α-helix | 324-331 | 8 | |
| 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 | 441-444 | 4 | |
| 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 | 473-489 | 17 | |
| α-helix | 491-494 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cryptochrome-1 | A | protein | 498 | Mus musculus | P97784 (AlphaFold model) |
>7D0M_1 Cryptochrome-1 (chains A) GTMGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQC LEDLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLAT EAGVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLVSKMEPLEMPADTITSDVIGKC MTPLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPR MNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYT AATNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLAR HAVACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGF GRRTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASR LNIERMKQIYQQLSRYRG
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 P97784 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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