Crystral Structure of the nucleoporin Nic96. Determined by X-ray diffraction at 2.6 Å resolution. Released 29 Jan 2008.
Explore 2RFO in 3D Show helices and sheets RCSB PDB PDBe
2RFO contains 73 α-helices and 15 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 | 207-228 | 22 | |
| α-helix | 234-244 | 11 | |
| α-helix | 250-261 | 12 | |
| α-helix | 270-290 | 21 | |
| α-helix | 301-310 | 10 | |
| β-strand | 315 | 1 | 1 |
| β-strand | 320 | 1 | 1 |
| β-strand | 327-328 | 2 | 2 |
| β-strand | 331-332 | 2 | 2 |
| α-helix | 333-342 | 10 | |
| α-helix | 346-355 | 10 | |
| α-helix | 357-359 | 3 | |
| α-helix | 365-374 | 10 | |
| α-helix | 388-393 | 6 | |
| α-helix | 394-398 | 5 | |
| α-helix | 406-416 | 11 | |
| 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 | 500-512 | 13 | |
| α-helix | 534-543 | 10 | |
| α-helix | 550-557 | 8 | |
| α-helix | 558-562 | 5 | |
| α-helix | 568-583 | 16 | |
| α-helix | 586-590 | 5 | |
| α-helix | 603-606 | 4 | |
| α-helix | 608-611 | 4 | |
| α-helix | 618-634 | 17 | |
| α-helix | 639-646 | 8 | |
| α-helix | 650-665 | 16 | |
| β-strand | 666 | 1 | 3 |
| α-helix | 685-696 | 12 | |
| α-helix | 700-703 | 4 | |
| α-helix | 708-725 | 18 | |
| α-helix | 732-741 | 10 | |
| α-helix | 750-753 | 4 | |
| α-helix | 755-758 | 4 | |
| α-helix | 771-774 | 4 | |
| α-helix | 778-784 | 7 | |
| α-helix | 808-819 | 12 | |
| α-helix | 831-834 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 208-226 | 19 | |
| α-helix | 234-242 | 9 | |
| α-helix | 248-263 | 16 | |
| α-helix | 270-288 | 19 | |
| α-helix | 304-310 | 7 | |
| β-strand | 314-315 | 2 | 4 |
| β-strand | 317-320 | 4 | 4 |
| β-strand | 327-328 | 2 | 5 |
| β-strand | 331-332 | 2 | 5 |
| α-helix | 333-341 | 9 | |
| α-helix | 346-354 | 9 | |
| α-helix | 357-359 | 3 | |
| α-helix | 366-370 | 5 | |
| β-strand | 371 | 1 | 6 |
| β-strand | 374 | 1 | 6 |
| α-helix | 385-393 | 9 | |
| α-helix | 394-398 | 5 | |
| α-helix | 406-416 | 11 | |
| α-helix | 432-442 | 11 | |
| α-helix | 460-469 | 10 | |
| α-helix | 471-474 | 4 | |
| α-helix | 478-484 | 7 | |
| α-helix | 488-496 | 9 | |
| α-helix | 500-512 | 13 | |
| α-helix | 534-543 | 10 | |
| α-helix | 550-558 | 9 | |
| α-helix | 559-562 | 4 | |
| α-helix | 566-583 | 18 | |
| β-strand | 591-593 | 3 | 7 |
| β-strand | 599-601 | 3 | 7 |
| α-helix | 603-606 | 4 | |
| α-helix | 608-610 | 3 | |
| α-helix | 620-632 | 13 | |
| β-strand | 638 | 1 | 8 |
| β-strand | 641 | 1 | 8 |
| α-helix | 642-646 | 5 | |
| α-helix | 652-665 | 14 | |
| α-helix | 685-696 | 12 | |
| α-helix | 700-703 | 4 | |
| α-helix | 708-728 | 21 | |
| α-helix | 732-741 | 10 | |
| α-helix | 750-757 | 8 | |
| α-helix | 765-768 | 4 | |
| α-helix | 771-785 | 15 | |
| α-helix | 805-818 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoporin NIC96 | A, B | protein | 651 | Saccharomyces cerevisiae | P34077 (AlphaFold model) |
>2RFO_1 Nucleoporin NIC96 (chains A, B) GNNILNSNESRLNVNENNILREKFENYARIVFQFNNSRQANGNFDIANEFISILSSANGT RNAQLLESWKILESMKSKDINIVEVGKQYLEQQFLQYTDNLYKKNMNEGLATNVNKIKSF IDTKLKKADKSWKISNLTVINGVPIWALIFYLLRAGLIKEALQVLVENKANIKKVEQSFL TYFKAYASSKDHGLPVEYSTKLHTEYNQHIKSSLDGDPYRLAVYKLIGRCDLSRKNIPAV TLSIEDWLWMHLMLIKEKDAENDPVYERYSLEDFQNIIISYGPSRFSNYYLQTLLLSGLY GLAIDYTYTFSEMDAVHLAIGLASLKLFKIDSSTRLTKKPKRDIRFANILANYTKSFRYS DPRVAVEYLVLITLNEGPTDVELCHEALRELVLETKEFTVLLGKIGRDGARIPGVIEERQ PLLHVRDEKEFLHTITEQAARRADEDGRIYDSILLYQLAEEYDIVITLVNSLLSDTLSAS DLDQPLVGPDDNSETNPVLLARRMASIYFDNAGISRQIHVKNKEICMLLLNISSIRELYF NKQWQETLSQMELLDLLPFSDELSARKKAQDFSNLDDNIVKNIPNLLIITLSCISNMIHI LNESKYQSSTKGQQIDSLKNVARQCMIYAGMIQYRMPRETYSTLINIDVSL
Structural basis of the nic96 subcomplex organization in the nuclear pore channel. Schrader, N., Stelter, P., Flemming, D. et al. Mol Cell (2008) 29:46-55. DOI 10.1016/j.molcel.2007.10.022 · PubMed
Other PDB entries of the same protein (UniProt P34077 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2RFO directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.