Nup84-Nup133 (aa521-1157) from S. cerevisiae bound by VHH-SAN8 and VHH-SAN9. Determined by X-ray diffraction at 7.3 Å resolution. Released 9 Dec 2020.
Explore 6X03 in 3D Show helices and sheets RCSB PDB PDBe
6X03 contains 84 α-helices and 21 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 | 11-25 | 15 | |
| α-helix | 37-40 | 4 | |
| α-helix | 42-52 | 11 | |
| α-helix | 59-61 | 3 | |
| α-helix | 62-84 | 23 | |
| α-helix | 117-127 | 11 | |
| α-helix | 135-136 | 2 | |
| α-helix | 173-187 | 15 | |
| α-helix | 188-190 | 3 | |
| α-helix | 193-202 | 10 | |
| α-helix | 206-208 | 3 | |
| α-helix | 209-224 | 16 | |
| α-helix | 246-250 | 5 | |
| α-helix | 258-268 | 11 | |
| α-helix | 274-276 | 3 | |
| α-helix | 284-286 | 3 | |
| α-helix | 287-305 | 19 | |
| α-helix | 324-334 | 11 | |
| α-helix | 336-339 | 4 | |
| α-helix | 346-349 | 4 | |
| α-helix | 383-399 | 17 | |
| α-helix | 406-419 | 14 | |
| α-helix | 430-432 | 3 | |
| α-helix | 448-450 | 3 | |
| α-helix | 457-461 | 5 | |
| α-helix | 470-475 | 6 | |
| α-helix | 477-480 | 4 | |
| α-helix | 486-491 | 6 | |
| α-helix | 503-506 | 4 | |
| α-helix | 509-511 | 3 | |
| α-helix | 512-516 | 5 | |
| α-helix | 531-533 | 3 | |
| α-helix | 543-552 | 10 | |
| α-helix | 557-563 | 7 | |
| α-helix | 576-601 | 26 | |
| α-helix | 612-636 | 25 | |
| α-helix | 637-639 | 3 | |
| α-helix | 647-658 | 12 | |
| α-helix | 661-668 | 8 | |
| α-helix | 669-671 | 3 | |
| α-helix | 674-676 | 3 | |
| α-helix | 681-689 | 9 | |
| α-helix | 694-696 | 3 | |
| α-helix | 712-719 | 8 | |
| α-helix | 720-723 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 520-538 | 19 | |
| α-helix | 554-571 | 18 | |
| α-helix | 580-592 | 13 | |
| α-helix | 595-607 | 13 | |
| α-helix | 609-626 | 18 | |
| α-helix | 642-656 | 15 | |
| α-helix | 662-676 | 15 | |
| α-helix | 708-712 | 5 | |
| α-helix | 718-729 | 12 | |
| α-helix | 737-745 | 9 | |
| α-helix | 748-769 | 22 | |
| α-helix | 776-798 | 23 | |
| α-helix | 804-811 | 8 | |
| α-helix | 816-823 | 8 | |
| α-helix | 831-838 | 8 | |
| α-helix | 839-841 | 3 | |
| α-helix | 845-848 | 4 | |
| α-helix | 849-852 | 4 | |
| α-helix | 870-872 | 3 | |
| α-helix | 873-876 | 4 | |
| α-helix | 885-888 | 4 | |
| α-helix | 896-909 | 14 | |
| α-helix | 916-930 | 15 | |
| α-helix | 942-966 | 25 | |
| α-helix | 983-992 | 10 | |
| α-helix | 994-997 | 4 | |
| α-helix | 1002-1007 | 6 | |
| α-helix | 1012-1016 | 5 | |
| α-helix | 1018-1024 | 7 | |
| α-helix | 1031-1051 | 21 | |
| α-helix | 1058-1067 | 10 | |
| α-helix | 1076-1079 | 4 | |
| α-helix | 1081-1084 | 4 | |
| α-helix | 1092-1098 | 7 | |
| α-helix | 1106-1123 | 18 | |
| α-helix | 1125-1127 | 3 | |
| α-helix | 1128-1140 | 13 | |
| β-strand | 1148-1149 | 2 | 1 |
| β-strand | 1154-1155 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 2 |
| β-strand | 10-13 | 4 | 3 |
| β-strand | 18-23 | 6 | 2 |
| β-strand | 37-39 | 3 | 3 |
| β-strand | 46-47 | 2 | 3 |
| β-strand | 65 | 1 | 2 |
| β-strand | 68-71 | 4 | 2 |
| β-strand | 78-83 | 6 | 2 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-95 | 4 | 3 |
| β-strand | 125-130 | 6 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 4 |
| β-strand | 10-13 | 4 | 5 |
| β-strand | 18-23 | 6 | 4 |
| β-strand | 37-39 | 3 | 5 |
| β-strand | 46-47 | 2 | 5 |
| β-strand | 68-71 | 4 | 4 |
| β-strand | 78-83 | 6 | 4 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-95 | 4 | 5 |
| β-strand | 122-127 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoporin NUP84 | A | protein | 726 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P52891 (AlphaFold model) |
| Nucleoporin NUP133 | B | protein | 643 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P36161 (AlphaFold model) |
| VHH-SAN8 | C | protein | 131 | Vicugna pacos | |
| VHH-SAN9 | D | protein | 128 | Vicugna pacos |
>6X03_1 Nucleoporin NUP84 (chains A) MELSPTYQTERFTKFSDTLKEFKIEQNNEQNPIDPFNIIREFRSAAGQLALDLANSGDES NVISSKDWELEARFWHLVELLLVFRNADLDLDEMELHPYNSRGLFEKKLMQDNKQLYQIW IVMVWLKENTYVMERPKNVPTSKWLNSITSGGLKSCDLDFPLRENTNVLDVKDKEEDHIF FKYIYELILAGAIDEALEEAKLSDNISICMILCGIQEYLNPVIDTQIANEFNTQQGIKKH SLWRRTVYSLSQQAGLDPYERAIYSYLSGAIPNQEVLQYSDWESDLHIHLNQILQTEIEN YLLENNQVGTDELILPLPSHALTVQEVLNRVASRHPSESEHPIRVLMASVILDSLPSVIH SSVEMLLDVVKGTEASNDIIDKPYLLRIVTHLAICLDIINPGSVEEVDKSKLITTYISLL KLQGLYENIPIYATFLNESDCLEACSFILSSLEDPQVRKKQIETINFLRLPASNILRRTT QRVFDETEQEYSPSNEISISFDVNNIDMHLIYGVEWLIEGKLYVDAVHSIIALSRRFLLN GRVKALEQFMERNNIGEICKNYELEKIADNISKDENEDQFLEEITQYEHLIKGIREYEEW QKSVSLLSSESNIPTLIEKLQGFSKDTFELIKTFLVDLTSSNFADSADYEILYEIRALYT PFLLMELHKKLVEAAKLLKIPKFISEALAFTSLVANENDKIYLLFQSSGKLKEYLDLVAR TATLSN
>6X03_2 Nucleoporin NUP133 (chains B) MADPGFSLDQESIEHDLKLTSEEIFHSNGKYIPPMLNTLGQHLSVRKEFFQNFLTFVAKN FNYKISPELKLDLIEKFEILNCCIKFNSIIRQSDVLNDIWEKTLSNYNLTQNEHLTTKTV VINSPDVFPVIFKQFLNHVVFVLFPSQNQNFKLNVTNLINLCFYDGILEEGEKTIRYELL ELDPMEVDTSKLPWFINFDYLNCINQCFFDFTFACEEEGSLDSYKEGLLKIVKILYYQFN QFKIWINTQPVKSVNANDNFININNLYDDNHLDWNHVLCKVNLKEQCIQIAEFYKDLSGL VQTLQTLDQNDSTTVSLYETFFNEFPKEFSFTLFEYLIKHKKLNDLIFRFPQQHDVLIQF FQESAPKYGHVAWIQQILDGSYADAMNTLKNITVDDSKKGESLSECELHLNVAKLSSLLV EKDNLDINTLRKIQYNLDTIDAEKNISNKLKKGEVQICKRFKNGSIREVFNILVEELKST TVVNLSDLVELYSMLDDEESLFIPLRLLSVDGNLLNFEVKKFLNALVWRRIVLLNASNEG DKLLQHIVKRVFDEELPKNNDFPLPSVDLLCDKSLLTPEYISETYGRFPIDQNAIREEIY EEISQVETLNSDNSLEIKLHSTIGSVAKEKNYTINYETNTVEY
>6X03_3 VHH-SAN8 (chains C) QLQLVETGGGLVQAGGSLRLSCVASGRTFTSYAMGWFRQAPGKEREFVAAISRLASGTDY ADSVKGRFTISRNNDKNTVYLQMNNLIPEDTAVYYCAALQALRFSLPIAMATMKNGRADS WGQGTQVTVSS
>6X03_4 VHH-SAN9 (chains D) QVQLVESGGGSVQAGGSLRLSCAVSGGTLSTLAMGWFRQAPGQEREFVARIGWTNGDTGY ADSVKGRFTISRDNVKNTVYLQMNNLKPEDTALYYCATRRPYGSTLYPPNTESAHDNWGQ GTQVTVSS
Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif. Nordeen, S.A., Turman, D.L., Schwartz, T.U. Nat Commun (2020) 11:6060-6060. DOI 10.1038/s41467-020-19885-5 · PubMed
Other PDB entries of the same protein (UniProt P52891 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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