Mammalian cryptochrome in complex with a small molecule competitor of its ubiquitin ligase. Determined by X-ray diffraction at 1.94 Å resolution. Released 16 Oct 2013.
Explore 4MLP in 3D Show helices and sheets RCSB PDB PDBe
4MLP contains 149 α-helices and 37 β-strands across 4 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 | 22-26 | 5 | 4 |
| α-helix | 37-43 | 7 | |
| β-strand | 48-55 | 8 | 4 |
| α-helix | 59-61 | 3 | |
| α-helix | 67-86 | 20 | |
| β-strand | 91-95 | 5 | 4 |
| α-helix | 98-109 | 12 | |
| 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 | 190-193 | 4 | |
| α-helix | 197-201 | 5 | |
| α-helix | 204-208 | 5 | |
| α-helix | 210-212 | 3 | |
| α-helix | 213-216 | 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 | 299-301 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 306-319 | 14 | |
| β-strand | 339 | 1 | 5 |
| α-helix | 342-349 | 8 | |
| α-helix | 356-368 | 13 | |
| α-helix | 373-381 | 9 | |
| α-helix | 382-386 | 5 | |
| β-strand | 390 | 1 | 5 |
| α-helix | 392-402 | 11 | |
| α-helix | 408-418 | 11 | |
| α-helix | 429-432 | 4 | |
| α-helix | 435-440 | 6 | |
| α-helix | 445-450 | 6 | |
| α-helix | 452-454 | 3 | |
| α-helix | 465-467 | 3 | |
| α-helix | 470-476 | 7 | |
| β-strand | 480 | 1 | 6 |
| β-strand | 484 | 1 | 6 |
| α-helix | 485-487 | 3 | |
| α-helix | 491-507 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-27 | 6 | 7 |
| α-helix | 37-43 | 7 | |
| β-strand | 48-55 | 8 | 7 |
| α-helix | 59-61 | 3 | |
| α-helix | 67-85 | 19 | |
| β-strand | 91-95 | 5 | 7 |
| α-helix | 98-109 | 12 | |
| β-strand | 113-117 | 5 | 7 |
| α-helix | 122-137 | 16 | |
| β-strand | 141-145 | 5 | 7 |
| α-helix | 153-159 | 7 | |
| α-helix | 168-176 | 9 | |
| α-helix | 179-189 | 11 | |
| α-helix | 190-195 | 6 | |
| α-helix | 197-201 | 5 | |
| α-helix | 204-208 | 5 | |
| α-helix | 210-212 | 3 | |
| α-helix | 213-216 | 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 | 299-301 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 306-318 | 13 | |
| β-strand | 339 | 1 | 8 |
| α-helix | 342-350 | 9 | |
| α-helix | 356-368 | 13 | |
| α-helix | 373-381 | 9 | |
| α-helix | 382-386 | 5 | |
| β-strand | 390 | 1 | 8 |
| α-helix | 392-402 | 11 | |
| α-helix | 408-418 | 11 | |
| α-helix | 429-432 | 4 | |
| α-helix | 435-440 | 6 | |
| α-helix | 445-450 | 6 | |
| α-helix | 452-454 | 3 | |
| α-helix | 465-467 | 3 | |
| α-helix | 470-476 | 7 | |
| β-strand | 480 | 1 | 9 |
| β-strand | 484 | 1 | 9 |
| α-helix | 485-487 | 3 | |
| α-helix | 491-507 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-26 | 5 | 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 | 98-109 | 12 | |
| β-strand | 113-117 | 5 | 1 |
| α-helix | 122-137 | 16 | |
| β-strand | 141-145 | 5 | 1 |
| α-helix | 153-159 | 7 | |
| α-helix | 168-176 | 9 | |
| α-helix | 179-189 | 11 | |
| α-helix | 190-194 | 5 | |
| α-helix | 197-201 | 5 | |
| α-helix | 204-208 | 5 | |
| α-helix | 209-212 | 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 | 299-301 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 306-318 | 13 | |
| β-strand | 339 | 1 | 2 |
| α-helix | 342-350 | 9 | |
| α-helix | 356-368 | 13 | |
| α-helix | 373-381 | 9 | |
| α-helix | 382-386 | 5 | |
| β-strand | 390 | 1 | 2 |
| α-helix | 392-402 | 11 | |
| α-helix | 408-418 | 11 | |
| α-helix | 429-432 | 4 | |
| 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 | 491-507 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-27 | 6 | 10 |
| α-helix | 37-43 | 7 | |
| β-strand | 48-55 | 8 | 10 |
| α-helix | 59-61 | 3 | |
| α-helix | 67-85 | 19 | |
| β-strand | 91-95 | 5 | 10 |
| α-helix | 98-109 | 12 | |
| β-strand | 113-117 | 5 | 10 |
| α-helix | 122-137 | 16 | |
| β-strand | 141-145 | 5 | 10 |
| α-helix | 153-159 | 7 | |
| α-helix | 168-176 | 9 | |
| α-helix | 179-189 | 11 | |
| α-helix | 190-195 | 6 | |
| β-strand | 197 | 1 | 10 |
| α-helix | 198-199 | 2 | |
| α-helix | 204-208 | 5 | |
| α-helix | 209-212 | 4 | |
| α-helix | 213-216 | 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 | 280-295 | 16 | |
| α-helix | 299-301 | 3 | |
| α-helix | 302-305 | 4 | |
| α-helix | 306-318 | 13 | |
| β-strand | 339 | 1 | 11 |
| α-helix | 342-350 | 9 | |
| α-helix | 356-368 | 13 | |
| α-helix | 373-381 | 9 | |
| α-helix | 382-386 | 5 | |
| β-strand | 390 | 1 | 11 |
| α-helix | 392-402 | 11 | |
| α-helix | 408-418 | 11 | |
| 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 | 470-476 | 7 | |
| β-strand | 480 | 1 | 12 |
| β-strand | 484 | 1 | 12 |
| α-helix | 485-487 | 3 | |
| α-helix | 491-507 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cryptochrome-2 | A, B, C, D | protein | 512 | Mus musculus | Q9R194 (AlphaFold model) |
>4MLP_1 Cryptochrome-2 (chains A, B, C, D) MAAAAVVAATVPAQSMGADGASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFA ASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDS EPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQALISRMEL PKKPAVAVSSQQMESCRAEIQENHDDTYGVPSLEELGFPTEGLGPAVWQGGETEALARLD KHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTP PLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDA IMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSC SAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKGFPSRYIYEPWNAPESVQKAAKCII GVDYPRPIVNHAETSRLNIERMKQIYQQLSRY
| ID | Name | Formula | Copies |
|---|---|---|---|
| 2CX | N-[(2S)-3-(9H-carbazol-9-yl)-2-hydroxypropyl]-N-(furan-2-ylmethyl)methanesulfon… | C21 H22 N2 O4 S | 4 |
Crystal structure of mammalian cryptochrome in complex with a small molecule competitor of its ubiquitin ligase. Nangle, S., Xing, W., Zheng, N. Cell Res (2013) 23:1417-1419. DOI 10.1038/cr.2013.136 · 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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