Kap95:Nup1 complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Oct 2017.
Explore 5OWU in 3D Show helices and sheets RCSB PDB PDBe
5OWU contains 65 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-35 | 17 | |
| α-helix | 37-48 | 12 | |
| α-helix | 55-67 | 13 | |
| α-helix | 74-87 | 14 | |
| α-helix | 90-104 | 15 | |
| α-helix | 109-126 | 18 | |
| α-helix | 127-129 | 3 | |
| α-helix | 133-142 | 10 | |
| α-helix | 149-165 | 17 | |
| α-helix | 174-176 | 3 | |
| α-helix | 177-188 | 12 | |
| α-helix | 195-208 | 14 | |
| α-helix | 209-211 | 3 | |
| α-helix | 213-216 | 4 | |
| α-helix | 219-233 | 15 | |
| α-helix | 238-255 | 18 | |
| α-helix | 256-258 | 3 | |
| α-helix | 260-262 | 3 | |
| α-helix | 263-267 | 5 | |
| α-helix | 268-274 | 7 | |
| α-helix | 280-306 | 27 | |
| α-helix | 317-332 | 16 | |
| α-helix | 347-362 | 16 | |
| α-helix | 363-366 | 4 | |
| α-helix | 367-377 | 11 | |
| α-helix | 383-395 | 13 | |
| α-helix | 402-418 | 17 | |
| α-helix | 419-421 | 3 | |
| α-helix | 425-442 | 18 | |
| α-helix | 443-445 | 3 | |
| α-helix | 452-463 | 12 | |
| α-helix | 467-484 | 18 | |
| α-helix | 491-495 | 5 | |
| α-helix | 496-507 | 12 | |
| α-helix | 513-515 | 3 | |
| α-helix | 516-530 | 15 | |
| α-helix | 533-535 | 3 | |
| α-helix | 536-553 | 18 | |
| α-helix | 558-560 | 3 | |
| α-helix | 563-586 | 24 | |
| α-helix | 588-590 | 3 | |
| α-helix | 592-594 | 3 | |
| α-helix | 595-607 | 13 | |
| α-helix | 611-613 | 3 | |
| α-helix | 615-629 | 15 | |
| α-helix | 630-636 | 7 | |
| α-helix | 637-649 | 13 | |
| α-helix | 655-669 | 15 | |
| α-helix | 671-674 | 4 | |
| α-helix | 675-689 | 15 | |
| α-helix | 698-713 | 16 | |
| α-helix | 714-717 | 4 | |
| α-helix | 718-732 | 15 | |
| α-helix | 734-736 | 3 | |
| α-helix | 741-764 | 24 | |
| α-helix | 769-772 | 4 | |
| α-helix | 773-775 | 3 | |
| α-helix | 776-788 | 13 | |
| α-helix | 790-793 | 4 | |
| α-helix | 796-812 | 17 | |
| α-helix | 819-821 | 3 | |
| α-helix | 825-836 | 12 | |
| α-helix | 842-860 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1004-1007 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-1 | A | protein | 861 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q06142 (AlphaFold model) |
| Nucleoporin NUP1 | B | protein | 1076 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P20676 (AlphaFold model) |
>5OWU_1 Importin subunit beta-1 (chains A) MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRIL AALTLKNELVSKDSVKTQQFAQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIA AIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALGYMCESADPQSQALVSSSNNI LIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEV QAAAFGCLCKIMSLYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDI AYELAQFPQSPLQSYNFALSSIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQ NCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGPDKVQRTYYVHQALPSILNLM NDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINL VEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSA SISTFVMDKLGQTMSVDENQLTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMG LFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETFSPYLLKALNQVDSPVSITAV GFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPY LNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIF QFIAQVAEDPQLYSEDATSRAAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLF SQATKDTARWAREQQKRQLSL
>5OWU_2 Nucleoporin NUP1 (chains B) MSSNTSSVMSSPRVEKRSFSSTLKSFFTNPNKKRPSSKKVFSSNLSYANHLEESDVEDTL HVNKRKRVSGTSQHSDSLTQNNNNAPIIIYGTENTERPPLLPILPIQRLRLLREKQRVRN MRELGLIQSTEFPSITSSVILGSQSKSDEGGSYLCTSSTPSPIKNGSCTRQLAGKSGEDT NVGLPILKSLKNRSNRKRFHSQSKGTVWSANFEYDLSEYDAIQKKDNKDKEGNAGGDQKT SENRNNIKSSISNGNLATGPNLTSEIEDLRADINSNRLSNPQKNLLLKGPASTVAKTAPI QESFVPNSERSGTPTLKKNIEPKKDKESIVLPTVGFDFIKDNETPSKKTSPKATSSAGAV FKSSVEMGKTDKSTKTAEAPTLSFNFSQKANKTKAVDNTVPSTTLFNFGGKSDTVTSASQ PFKFGKTSEKSENHTESDAPPKSTAPIFSFGKQEENGDEGDDENEPKRKRRLPVSEDTNT KPLFDFGKTGDQKETKKGESEKDASGKPSFVFGASDKQAEGTPLFTFGKKADVTSNIDSS AQFTFGKAATAKETHTKPSETPATIVKKPTFTFGQSTSENKISEGSAKPTFSFSKSEEER KSSPISNEAAKPSFSFPGKPVDVQAPTDDKTLKPTFSFTEPAQKDSSVVSEPKKPSFTFA SSKTSQPKPLFSFGKSDAAKEPPGSNTSFSFTKPPANETDKRPTPPSFTFGGSTTNNTTT TSTKPSFSFGAPESMKSTASTAAANTEKLSNGFSFTKFNHNKEKSNSPTSFFDGSASSTP IPVLGKPTDATGNTTSKSAFSFGTANTNGTNASANSTSFSFNAPATGNGTTTTSNTSGTN IAGTFNVGKPDQSIASGNTNGAGSAFGFSSSGTAATGAASNQSSFNFGNNGAGGLNPFTS ATSSTNANAGLFNKPPSTNAQNVNVPSAFNFTGNNSTPGGGSVFNMNGNTNANTVFAGSN NQPHQSQTPSFNTNSSFTPSTVPNINFSGLNGGITNTATNALRPSDIFGANAASGSNSNV TNPSSIFGGAGGVPTTSFGQPQSAPNQMGMGTNNGMSMGGGVMANRKIARMRHSKR
Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p. Liu, S.M., Stewart, M. J Mol Biol (2005) 349:515-525. DOI 10.1016/j.jmb.2005.04.003 · PubMed
Other PDB entries of the same protein (UniProt Q06142 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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