Crystal Structure of Mouse Cryptochrome1 in Complex with Period2. Determined by X-ray diffraction at 2.45 Å resolution. Released 4 Jun 2014.
Explore 4CT0 in 3D Show helices and sheets RCSB PDB PDBe
4CT0 contains 38 α-helices and 12 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 | 4-9 | 6 | 1 |
| α-helix | 19-24 | 6 | |
| β-strand | 30-37 | 8 | 1 |
| α-helix | 49-68 | 20 | |
| β-strand | 73-77 | 5 | 1 |
| α-helix | 80-91 | 12 | |
| β-strand | 93-99 | 7 | 1 |
| α-helix | 104-118 | 15 | |
| β-strand | 123-127 | 5 | 1 |
| α-helix | 135-141 | 7 | |
| α-helix | 150-158 | 9 | |
| α-helix | 161-169 | 9 | |
| α-helix | 172-175 | 4 | |
| β-strand | 179 | 1 | 1 |
| α-helix | 195-198 | 4 | |
| α-helix | 206-208 | 3 | |
| α-helix | 214-231 | 18 | |
| α-helix | 246-247 | 2 | |
| α-helix | 252-257 | 6 | |
| α-helix | 262-276 | 15 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-300 | 13 | |
| β-strand | 321 | 1 | 2 |
| 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 | 411-414 | 4 | |
| α-helix | 417-422 | 6 | |
| α-helix | 427-432 | 6 | |
| α-helix | 434-436 | 3 | |
| α-helix | 447-449 | 3 | |
| α-helix | 454-458 | 5 | |
| β-strand | 462 | 1 | 3 |
| β-strand | 466 | 1 | 3 |
| α-helix | 467-469 | 3 | |
| α-helix | 473-494 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | -8--5 | 4 | 4 |
| β-strand | 1132-1135 | 4 | 4 |
| α-helix | 1138-1141 | 4 | |
| α-helix | 1147-1152 | 6 | |
| α-helix | 1155-1157 | 3 | |
| α-helix | 1160-1174 | 15 | |
| α-helix | 1175-1177 | 3 | |
| α-helix | 1183-1190 | 8 | |
| α-helix | 1195-1198 | 4 | |
| α-helix | 1203-1205 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cryptochrome-1 | A | protein | 507 | MUS MUSCULUS | P97784 (AlphaFold model) |
| Period circadian protein homolog 2 | B | protein | 143 | MUS MUSCULUS | O54943 (AlphaFold model) |
>4CT0_1 CRYPTOCHROME-1 (chains A) MGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQCLE DLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLATEA GVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLVSKMEPLEMPADTITSDVIGKCMT PLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPRMN ANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYTAA TNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHA VACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGFGR RTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASRLN IERMKQIYQQLSRYRGAAALEHHHHHH
>4CT0_2 PERIOD CIRCADIAN PROTEIN HOMOLOG 2 (chains B) MKHHHHHHSAGLEVLFQGPDSMYVLQDPIWLLMANTDDSIMMTYQLPSRDLQAVLKEDQE KLKLLQRSQPRFTEGQRRELREVHPWVHTGGLPTAIDVTGCVYCESEEKGNICLPYEEDS PSPGLCDTSEAKEEEGEQLTGPR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (P6G, CL) are not listed.
Interaction of Circadian Clock Proteins Cry1 and Per2 is Modulated by Zinc Binding and Disulfide Bond Formation. Schmalen, I., Reischl, S., Wallach, T. et al. Cell (2014) 157:1203. DOI 10.1016/J.CELL.2014.03.057 · 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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