Structure of nucleoporin Nic96. Determined by X-ray diffraction at 2.5 Å resolution. Released 25 Sept 2007.
Explore 2QX5 in 3D Show helices and sheets RCSB PDB PDBe
2QX5 contains 78 α-helices and 12 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 | 206-227 | 22 | |
| α-helix | 234-243 | 10 | |
| α-helix | 248-261 | 14 | |
| α-helix | 270-293 | 24 | |
| α-helix | 301-311 | 11 | |
| β-strand | 314 | 1 | 1 |
| β-strand | 320 | 1 | 1 |
| β-strand | 327-328 | 2 | 2 |
| β-strand | 331-332 | 2 | 2 |
| α-helix | 333-341 | 9 | |
| α-helix | 346-355 | 10 | |
| α-helix | 357-359 | 3 | |
| α-helix | 367-373 | 7 | |
| α-helix | 406-412 | 7 | |
| α-helix | 413-417 | 5 | |
| α-helix | 420-422 | 3 | |
| α-helix | 426-428 | 3 | |
| α-helix | 432-441 | 10 | |
| α-helix | 459-469 | 11 | |
| α-helix | 471-474 | 4 | |
| α-helix | 478-484 | 7 | |
| α-helix | 488-496 | 9 | |
| α-helix | 500-512 | 13 | |
| α-helix | 534-542 | 9 | |
| α-helix | 550-558 | 9 | |
| α-helix | 559-562 | 4 | |
| α-helix | 566-583 | 18 | |
| α-helix | 586-590 | 5 | |
| β-strand | 592-593 | 2 | 3 |
| β-strand | 599-600 | 2 | 3 |
| α-helix | 603-606 | 4 | |
| α-helix | 609-611 | 3 | |
| α-helix | 616-633 | 18 | |
| α-helix | 637-646 | 10 | |
| α-helix | 650-667 | 18 | |
| α-helix | 685-696 | 12 | |
| α-helix | 700-703 | 4 | |
| α-helix | 708-728 | 21 | |
| α-helix | 732-741 | 10 | |
| α-helix | 754-759 | 6 | |
| α-helix | 760-762 | 3 | |
| α-helix | 765-768 | 4 | |
| α-helix | 771-790 | 20 | |
| α-helix | 799-819 | 21 | |
| α-helix | 821-823 | 3 | |
| α-helix | 826-833 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 206-228 | 23 | |
| α-helix | 234-243 | 10 | |
| α-helix | 248-261 | 14 | |
| α-helix | 270-290 | 21 | |
| α-helix | 301-311 | 11 | |
| β-strand | 314-315 | 2 | 4 |
| β-strand | 319-320 | 2 | 4 |
| β-strand | 328 | 1 | 5 |
| β-strand | 331 | 1 | 5 |
| α-helix | 333-341 | 9 | |
| α-helix | 346-354 | 9 | |
| α-helix | 367-373 | 7 | |
| α-helix | 406-416 | 11 | |
| α-helix | 420-422 | 3 | |
| α-helix | 432-442 | 11 | |
| α-helix | 459-469 | 11 | |
| α-helix | 471-473 | 3 | |
| α-helix | 478-484 | 7 | |
| α-helix | 488-496 | 9 | |
| α-helix | 500-511 | 12 | |
| α-helix | 534-541 | 8 | |
| α-helix | 542-545 | 4 | |
| α-helix | 550-559 | 10 | |
| α-helix | 560-562 | 3 | |
| α-helix | 568-583 | 16 | |
| α-helix | 586-590 | 5 | |
| β-strand | 592-593 | 2 | 6 |
| β-strand | 599-600 | 2 | 6 |
| α-helix | 603-606 | 4 | |
| α-helix | 609-611 | 3 | |
| α-helix | 619-634 | 16 | |
| α-helix | 637-646 | 10 | |
| α-helix | 650-667 | 18 | |
| α-helix | 685-696 | 12 | |
| α-helix | 700-703 | 4 | |
| α-helix | 708-728 | 21 | |
| α-helix | 732-741 | 10 | |
| α-helix | 754-759 | 6 | |
| α-helix | 760-762 | 3 | |
| α-helix | 765-768 | 4 | |
| α-helix | 771-790 | 20 | |
| α-helix | 799-819 | 21 | |
| α-helix | 821-823 | 3 | |
| α-helix | 826-831 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoporin NIC96 | A, B | protein | 661 | Saccharomyces cerevisiae | P34077 (AlphaFold model) |
>2QX5_1 Nucleoporin NIC96 (chains A, B) PGSEFELGNKGNNILNSNESRLNVNENNILREKFENYARIVFQFNNSRQANGNFDIANEF ISILSSANGTRNAQLLESWKILESMKSKDINIVEVGKQYLEQQFLQYTDNLYKKNMNEGL ATNVNKIKSFIDTKLKKADKSWKISNLTVINGVPIWALIFYLLRAGLIKEALQVLVENKA NIKKVEQSFLTYFKAYASSKDHGLPVEYSTKLHTEYNQHIKSSLDGDPYRLAVYKLIGRC DLSRKNIPAVTLSIEDWLWMHLMLIKEKDAENDPVYERYSLEDFQNIIISYGPSRFSNYY LQTLLLSGLYGLAIDYTYTFSEMDAVHLAIGLASLKLFKIDSSTRLTKKPKRDIRFANIL ANYTKSFRYSDPRVAVEYLVLITLNEGPTDVELCHEALRELVLETKEFTVLLGKIGRDGA RIPGVIEERQPLLHVRDEKEFLHTITEQAARRADEDGRIYDSILLYQLAEEYDIVITLVN SLLSDTLSASDLDQPLVGPDDNSETNPVLLARRMASIYFDNAGISRQIHVKNKEICMLLL NISSIRELYFNKQWQETLSQMELLDLLPFSDELSARKKAQDFSNLDDNIVKNIPNLLIIT LSCISNMIHILNESKYQSSTKGQQIDSLKNVARQCMIYAGMIQYRMPRETYSTLINIDVS L
Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture. Jeudy, S., Schwartz, T.U. J Biol Chem (2007) 282:34904. DOI 10.1074/jbc.M705479200 · PubMed
Other PDB entries of the same protein (UniProt P34077 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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