Transportin 3 in complex with phosphorylated ASF/SF2. Determined by X-ray diffraction at 2.56 Å resolution. Released 22 Jan 2014.
Explore 4C0O in 3D Show helices and sheets RCSB PDB PDBe
4C0O contains 130 α-helices and 12 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 |
|---|---|---|---|
| α-helix | 4-7 | 4 | |
| α-helix | 8-20 | 13 | |
| α-helix | 24-39 | 16 | |
| α-helix | 43-53 | 11 | |
| α-helix | 57-73 | 17 | |
| α-helix | 75-77 | 3 | |
| α-helix | 82-96 | 15 | |
| α-helix | 102-117 | 16 | |
| α-helix | 125-133 | 9 | |
| α-helix | 140-152 | 13 | |
| α-helix | 153-155 | 3 | |
| α-helix | 163-188 | 26 | |
| α-helix | 195-211 | 17 | |
| α-helix | 216-220 | 5 | |
| α-helix | 223-233 | 11 | |
| α-helix | 239-254 | 16 | |
| α-helix | 263-274 | 12 | |
| α-helix | 277-285 | 9 | |
| α-helix | 289-305 | 17 | |
| α-helix | 307-312 | 6 | |
| α-helix | 317-319 | 3 | |
| α-helix | 322-331 | 10 | |
| α-helix | 336-339 | 4 | |
| α-helix | 340-342 | 3 | |
| α-helix | 343-355 | 13 | |
| α-helix | 362-364 | 3 | |
| α-helix | 366-379 | 14 | |
| α-helix | 381-383 | 3 | |
| α-helix | 395-410 | 16 | |
| α-helix | 411-413 | 3 | |
| α-helix | 416-425 | 10 | |
| α-helix | 434-447 | 14 | |
| α-helix | 456-467 | 12 | |
| α-helix | 475-487 | 13 | |
| α-helix | 490-494 | 5 | |
| α-helix | 496-498 | 3 | |
| α-helix | 499-510 | 12 | |
| α-helix | 513-515 | 3 | |
| α-helix | 516-529 | 14 | |
| α-helix | 538-546 | 9 | |
| α-helix | 548-550 | 3 | |
| α-helix | 555-569 | 15 | |
| α-helix | 574-595 | 22 | |
| α-helix | 609-621 | 13 | |
| α-helix | 635-651 | 17 | |
| α-helix | 656-673 | 18 | |
| α-helix | 681-694 | 14 | |
| α-helix | 698-711 | 14 | |
| α-helix | 718-737 | 20 | |
| α-helix | 741-744 | 4 | |
| α-helix | 746-762 | 17 | |
| α-helix | 764-768 | 5 | |
| α-helix | 773-783 | 11 | |
| α-helix | 789-803 | 15 | |
| α-helix | 804-806 | 3 | |
| α-helix | 815-839 | 25 | |
| α-helix | 840-844 | 5 | |
| α-helix | 847-849 | 3 | |
| α-helix | 850-877 | 28 | |
| α-helix | 892-903 | 12 | |
| α-helix | 908-919 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-7 | 4 | |
| α-helix | 8-20 | 13 | |
| α-helix | 24-39 | 16 | |
| α-helix | 43-53 | 11 | |
| α-helix | 57-73 | 17 | |
| α-helix | 75-77 | 3 | |
| α-helix | 80-96 | 17 | |
| α-helix | 102-117 | 16 | |
| α-helix | 125-133 | 9 | |
| α-helix | 140-152 | 13 | |
| α-helix | 153-155 | 3 | |
| α-helix | 163-175 | 13 | |
| α-helix | 177-188 | 12 | |
| α-helix | 195-211 | 17 | |
| α-helix | 216-220 | 5 | |
| α-helix | 223-231 | 9 | |
| α-helix | 239-255 | 17 | |
| α-helix | 263-274 | 12 | |
| α-helix | 277-285 | 9 | |
| α-helix | 289-305 | 17 | |
| α-helix | 307-312 | 6 | |
| α-helix | 317-319 | 3 | |
| α-helix | 322-331 | 10 | |
| α-helix | 336-339 | 4 | |
| α-helix | 340-342 | 3 | |
| α-helix | 343-355 | 13 | |
| α-helix | 362-379 | 18 | |
| α-helix | 381-383 | 3 | |
| α-helix | 395-410 | 16 | |
| α-helix | 411-413 | 3 | |
| α-helix | 416-425 | 10 | |
| α-helix | 434-447 | 14 | |
| α-helix | 456-467 | 12 | |
| α-helix | 475-487 | 13 | |
| α-helix | 489-494 | 6 | |
| α-helix | 496-498 | 3 | |
| α-helix | 499-510 | 12 | |
| α-helix | 513-515 | 3 | |
| α-helix | 516-529 | 14 | |
| α-helix | 538-546 | 9 | |
| α-helix | 548-550 | 3 | |
| α-helix | 555-569 | 15 | |
| α-helix | 574-595 | 22 | |
| α-helix | 609-621 | 13 | |
| α-helix | 635-651 | 17 | |
| α-helix | 656-673 | 18 | |
| α-helix | 681-694 | 14 | |
| α-helix | 698-711 | 14 | |
| α-helix | 718-737 | 20 | |
| α-helix | 741-744 | 4 | |
| α-helix | 746-762 | 17 | |
| α-helix | 764-768 | 5 | |
| α-helix | 773-783 | 11 | |
| α-helix | 789-803 | 15 | |
| α-helix | 804-806 | 3 | |
| α-helix | 815-839 | 25 | |
| α-helix | 840-844 | 5 | |
| α-helix | 847-849 | 3 | |
| α-helix | 850-877 | 28 | |
| α-helix | 892-903 | 12 | |
| α-helix | 908-920 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 122-126 | 5 | 1 |
| α-helix | 134-141 | 8 | |
| β-strand | 147-152 | 6 | 1 |
| β-strand | 158-162 | 5 | 1 |
| α-helix | 165-170 | 6 | |
| α-helix | 171-175 | 5 | |
| β-strand | 179-181 | 3 | 2 |
| β-strand | 187-189 | 3 | 2 |
| β-strand | 191-194 | 4 | 1 |
| α-helix | 198-200 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-3 | A, B | protein | 923 | HOMO SAPIENS | Q9Y5L0 (AlphaFold model) |
| Serine/arginine-rich splicing factor 1 | C, D | protein | 125 | HOMO SAPIENS | Q07955 (AlphaFold model) |
>4C0O_1 TRANSPORTIN-3 (chains A, B) MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESC YFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMP SWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTV VSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSN LHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFT ELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEV IHGIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECF AQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYT SIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNG LLEIARSLDSFLLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEP SNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVE RCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQG LLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWA IASTTLDHRDANCSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHT CCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHK QVTSAEECKQVCWALRDFTRLFR
>4C0O_2 SERINE/ARGININE-RICH SPLICING FACTOR 1 (chains C, D) GAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRK EDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRS YSPRR
Structural Basis for Nuclear Import of Splicing Factors by Human Transportin 3. Maertens, G.N., Cook, N.J., Wang, W. et al. Proc Natl Acad Sci U S A (2014) 111:2728. DOI 10.1073/PNAS.1320755111 · PubMed
Other PDB entries of the same protein (UniProt Q9Y5L0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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