Crystal structure of Kap121p mutant D353K/E396K/D438K. Determined by X-ray diffraction at 3.2 Å resolution. Released 10 Apr 2013.
Explore 3W3V in 3D Show helices and sheets RCSB PDB PDBe
3W3V contains 70 α-helices and 3 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 |
|---|---|---|---|
| α-helix | 6-19 | 14 | |
| α-helix | 25-37 | 13 | |
| α-helix | 44-57 | 14 | |
| α-helix | 61-77 | 17 | |
| α-helix | 91-93 | 3 | |
| α-helix | 96-111 | 16 | |
| α-helix | 116-127 | 12 | |
| α-helix | 135-136 | 2 | |
| α-helix | 138-149 | 12 | |
| α-helix | 153-165 | 13 | |
| α-helix | 168-172 | 5 | |
| α-helix | 175-187 | 13 | |
| α-helix | 191-207 | 17 | |
| α-helix | 210-215 | 6 | |
| α-helix | 217-219 | 3 | |
| α-helix | 220-225 | 6 | |
| α-helix | 228-232 | 5 | |
| α-helix | 236-252 | 17 | |
| α-helix | 254-257 | 4 | |
| α-helix | 261-273 | 13 | |
| α-helix | 279-295 | 17 | |
| α-helix | 297-301 | 5 | |
| α-helix | 304-317 | 14 | |
| α-helix | 329-332 | 4 | |
| α-helix | 343-376 | 34 | |
| α-helix | 381-394 | 14 | |
| α-helix | 399-402 | 4 | |
| α-helix | 406-413 | 8 | |
| α-helix | 414-418 | 5 | |
| α-helix | 422-438 | 17 | |
| α-helix | 442-459 | 18 | |
| α-helix | 465-479 | 15 | |
| α-helix | 484-487 | 4 | |
| α-helix | 488-490 | 3 | |
| α-helix | 491-502 | 12 | |
| α-helix | 507-524 | 18 | |
| α-helix | 525-528 | 4 | |
| α-helix | 529-544 | 16 | |
| α-helix | 551-568 | 18 | |
| α-helix | 570-573 | 4 | |
| α-helix | 577-588 | 12 | |
| α-helix | 596-613 | 18 | |
| α-helix | 614-620 | 7 | |
| α-helix | 621-631 | 11 | |
| β-strand | 638-640 | 3 | 1 |
| α-helix | 644-646 | 3 | |
| α-helix | 649-651 | 3 | |
| β-strand | 656-661 | 6 | 1 |
| β-strand | 663-667 | 5 | 1 |
| α-helix | 669-689 | 21 | |
| α-helix | 690-693 | 4 | |
| α-helix | 694-700 | 7 | |
| α-helix | 701-705 | 5 | |
| α-helix | 706-708 | 3 | |
| α-helix | 715-735 | 21 | |
| α-helix | 742-760 | 19 | |
| α-helix | 764-781 | 18 | |
| α-helix | 788-809 | 22 | |
| α-helix | 830-849 | 20 | |
| α-helix | 853-858 | 6 | |
| α-helix | 861-868 | 8 | |
| α-helix | 873-888 | 16 | |
| α-helix | 895-909 | 15 | |
| α-helix | 914-930 | 17 | |
| α-helix | 936-949 | 14 | |
| α-helix | 961-977 | 17 | |
| α-helix | 987-993 | 7 | |
| α-helix | 1002-1017 | 16 | |
| α-helix | 1029-1041 | 13 | |
| α-helix | 1053-1062 | 10 | |
| α-helix | 1066-1070 | 5 | |
| α-helix | 1071-1074 | 4 | |
| α-helix | 1078-1085 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-3 | A | protein | 1078 | Saccharomyces cerevisiae | P32337 (AlphaFold model) |
>3W3V_1 Importin subunit beta-3 (chains A) MSALPEEVNRTLLQIVQAFASPDNQIRSVAEKALSEEWITENNIEYLLTFLAEQAAFSQD TTVAALSAVLFRKLALKAPITHIRKEVLAQIRSSLLKGFLSERADSIRHKLSDAIAECVQ DDLPAWPELLQALIESLKSGNPNFRESSFRILTTVPYLITAVDINSILPIFQSGFTDASD NVKIAAVTAFVGYFKQLPKSEWSKLGILLPSLLNSLPRFLDDGKDDALASVFESLIELVE LAPKLFKDMFDQIIQFTDMVIKNKDLEPPARTTALELLTVFSENAPQMCKSNQNYGQTLV MVTLIMMTEVSIDDDDAAEWIESDDTDDEEEVTYDHARQALKRVALKLGGEYLAAPLFQY LQQMITSTEWRERFAAMMALSSAAKGCADVLIGEIPKILDMVIPLINDPHPRVQYGCCNV LGQISTKFSPFIQRTAHDRILPALISKLTSECTSRVQTHAAAALVNFSEFASKDILEPYL DSLLTNLLVLLQSNKLYVQEQALTTIAFIAEAAKNKFIKYYDTLMPLLLNVLKVNNKDNS VLKGKCMECATLIGFAVGKEKFHEHSQELISILVALQNSDIDEDDALRSYLEQSWSRICR ILGDDFVPLLPIVIPPLLITAKATQDVGLIEEEEAANFQQYPDWDVVQVQGKHIAIHTSV LDDKVSAMELLQSYATLLRGQFAVYVKEVMEEIALPSLDFYLHDGVRAAGATLIPILLSC LLAATGTQNEELVLLWHKASSKLIGGLMSEPMPEITQVYHNSLVNGIKVMGDNCLSEDQL AAFTKGVSANLTDTYERMQDRHGDGDEYNENIDEEEDFTDEDLLDEINKSIAAVLKTTNG HYLKNLENIWPMINTFLLDNEPILVIFALVVIGDLIQYGGEQTASMKNAFIPKVTECLIS PDARIRQAASYIIGVCAQYAPSTYADVCIPTLDTLVQIVDFPGSKLEENRSSTENASAAI AKILYAYNSNIPNVDTYTANWFKTLPTITDKEAASFNYQFLSQLIENNSPIVCAQSNISA VVDSVIQALNERSLTEREGQTVISSVKKLLGFLPSSDAMAIFNRYPADIMEKVHKWFA
Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p. Kobayashi, J., Matsuura, Y. J Mol Biol (2013) 425:1852-1868. DOI 10.1016/j.jmb.2013.02.035 · PubMed
Other PDB entries of the same protein (UniProt P32337 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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