Transportin-3 TNPO3 in complex with RSY region of CIRBP. Determined by X-ray diffraction at 2.94 Å resolution. Released 6 Mar 2024.
Explore 8CMK in 3D Show helices and sheets RCSB PDB PDBe
8CMK contains 119 α-helices and 0 β-strands across 5 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 | 57-74 | 18 | |
| α-helix | 75-77 | 3 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-96 | 14 | |
| α-helix | 102-118 | 17 | |
| α-helix | 125-133 | 9 | |
| α-helix | 140-153 | 14 | |
| α-helix | 163-175 | 13 | |
| α-helix | 177-189 | 13 | |
| α-helix | 195-210 | 16 | |
| α-helix | 216-220 | 5 | |
| α-helix | 224-233 | 10 | |
| α-helix | 239-254 | 16 | |
| α-helix | 259-261 | 3 | |
| α-helix | 263-285 | 23 | |
| α-helix | 289-305 | 17 | |
| α-helix | 307-312 | 6 | |
| α-helix | 317-319 | 3 | |
| α-helix | 322-330 | 9 | |
| α-helix | 336-339 | 4 | |
| α-helix | 343-355 | 13 | |
| α-helix | 359-379 | 21 | |
| α-helix | 381-383 | 3 | |
| α-helix | 389-391 | 3 | |
| α-helix | 397-414 | 18 | |
| α-helix | 416-428 | 13 | |
| α-helix | 434-448 | 15 | |
| α-helix | 456-468 | 13 | |
| α-helix | 475-487 | 13 | |
| α-helix | 489-494 | 6 | |
| α-helix | 496-498 | 3 | |
| α-helix | 499-510 | 12 | |
| α-helix | 513-529 | 17 | |
| α-helix | 531-536 | 6 | |
| α-helix | 538-546 | 9 | |
| α-helix | 548-550 | 3 | |
| α-helix | 555-569 | 15 | |
| α-helix | 577-597 | 21 | |
| α-helix | 609-621 | 13 | |
| α-helix | 633-651 | 19 | |
| α-helix | 656-672 | 17 | |
| α-helix | 674-679 | 6 | |
| α-helix | 681-694 | 14 | |
| α-helix | 698-711 | 14 | |
| α-helix | 715-736 | 22 | |
| α-helix | 741-744 | 4 | |
| α-helix | 746-762 | 17 | |
| α-helix | 764-768 | 5 | |
| α-helix | 773-783 | 11 | |
| α-helix | 789-804 | 16 | |
| α-helix | 816-839 | 24 | |
| α-helix | 840-844 | 5 | |
| α-helix | 847-849 | 3 | |
| α-helix | 850-878 | 29 | |
| α-helix | 892-903 | 12 | |
| α-helix | 908-919 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-15 | 3 | |
| α-helix | 27-37 | 11 | |
| α-helix | 60-74 | 15 | |
| α-helix | 84-96 | 13 | |
| α-helix | 102-116 | 15 | |
| α-helix | 126-133 | 8 | |
| α-helix | 140-153 | 14 | |
| α-helix | 163-189 | 27 | |
| α-helix | 195-210 | 16 | |
| α-helix | 218-221 | 4 | |
| α-helix | 224-233 | 10 | |
| α-helix | 239-254 | 16 | |
| α-helix | 265-274 | 10 | |
| α-helix | 277-285 | 9 | |
| α-helix | 289-312 | 24 | |
| α-helix | 317-319 | 3 | |
| α-helix | 322-330 | 9 | |
| α-helix | 336-339 | 4 | |
| α-helix | 340-342 | 3 | |
| α-helix | 343-356 | 14 | |
| α-helix | 359-379 | 21 | |
| α-helix | 381-383 | 3 | |
| α-helix | 389-391 | 3 | |
| α-helix | 395-414 | 20 | |
| α-helix | 416-427 | 12 | |
| α-helix | 434-447 | 14 | |
| α-helix | 458-467 | 10 | |
| α-helix | 475-487 | 13 | |
| α-helix | 489-494 | 6 | |
| α-helix | 496-498 | 3 | |
| α-helix | 499-510 | 12 | |
| α-helix | 513-529 | 17 | |
| α-helix | 538-546 | 9 | |
| α-helix | 548-550 | 3 | |
| α-helix | 555-569 | 15 | |
| α-helix | 574-596 | 23 | |
| α-helix | 609-621 | 13 | |
| α-helix | 631-632 | 2 | |
| α-helix | 635-651 | 17 | |
| α-helix | 656-671 | 16 | |
| α-helix | 674-677 | 4 | |
| α-helix | 678-694 | 17 | |
| α-helix | 699-711 | 13 | |
| α-helix | 715-736 | 22 | |
| α-helix | 741-744 | 4 | |
| α-helix | 746-762 | 17 | |
| α-helix | 764-768 | 5 | |
| α-helix | 773-783 | 11 | |
| α-helix | 789-804 | 16 | |
| α-helix | 816-839 | 24 | |
| α-helix | 840-844 | 5 | |
| α-helix | 847-849 | 3 | |
| α-helix | 850-878 | 29 | |
| α-helix | 892-903 | 12 | |
| α-helix | 908-919 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 160-164 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 160-163 | 4 | |
| α-helix | 167-170 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 155-162 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-3 | A, B | protein | 923 | Homo sapiens | Q9Y5L0 (AlphaFold model) |
| Cold-inducible RNA-binding protein | C, D, E | protein | 35 | Homo sapiens | Q14011 (AlphaFold model) |
>8CMK_1 Transportin-3 (chains A, B) MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESC YFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMP SWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTV VSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSN LHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFT ELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEV IHGIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECF AQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYT SIELVGEMSEVVDRNPQFLDPVLGYLMKGLAEKPLASAAAKAIHNICSVCRDHMAQHFNG LLEIARSLDSFLLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEP SNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVE RCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQG LLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWA IASTTLDHRDANCSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHT CCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHK QVTSAEECKQVCWALRDFTRLFR
>8CMK_2 Cold-inducible RNA-binding protein (chains C, D, E) SRDYYSSRSQSGGYSDRSSGGSYRDSYDSYATHNE
| ID | Name | Formula | Copies |
|---|---|---|---|
| TSS | 2-(1H-indol-3-yl)ethanamine | C10 H12 N2 | 1 |
Water and common crystallization additives (PEG) are not listed.
Structural basis of phosphorylation-independent nuclear import of CIRBP by TNPO3. Zhou, Q., Sagmeister, T., Hutten, S. et al. Nat Commun (2025) 16:4456-4456. DOI 10.1038/s41467-025-59802-2 · 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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