Crystal structure of Kap60 bound to yeast RCC1 (Prp20). Determined by X-ray diffraction at 2.63 Å resolution. Released 13 Sept 2017.
Explore 5T94 in 3D Show helices and sheets RCSB PDB PDBe
5T94 contains 43 α-helices and 33 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 | 33-35 | 3 | |
| α-helix | 37-40 | 4 | |
| β-strand | 47-53 | 7 | 1 |
| α-helix | 65-67 | 3 | |
| β-strand | 69-75 | 7 | 1 |
| β-strand | 86-91 | 6 | 2 |
| β-strand | 95-100 | 6 | 2 |
| β-strand | 105-109 | 5 | 2 |
| α-helix | 145-148 | 4 | |
| β-strand | 151-152 | 2 | 2 |
| α-helix | 153-154 | 2 | |
| α-helix | 155-157 | 3 | |
| α-helix | 159-162 | 4 | |
| β-strand | 167-172 | 6 | 3 |
| β-strand | 176-181 | 6 | 3 |
| β-strand | 186-190 | 5 | 3 |
| β-strand | 192-193 | 2 | 4 |
| β-strand | 198-200 | 3 | 4 |
| β-strand | 202 | 1 | 5 |
| β-strand | 206 | 1 | 5 |
| β-strand | 209-215 | 7 | 3 |
| α-helix | 216-217 | 2 | |
| β-strand | 223-228 | 6 | 6 |
| β-strand | 232-237 | 6 | 6 |
| β-strand | 242-246 | 5 | 6 |
| β-strand | 269-270 | 2 | 6 |
| β-strand | 276-281 | 6 | 7 |
| β-strand | 285-290 | 6 | 7 |
| β-strand | 295-300 | 6 | 7 |
| β-strand | 317-323 | 7 | 7 |
| β-strand | 332-337 | 6 | 8 |
| β-strand | 341-346 | 6 | 8 |
| β-strand | 351-356 | 6 | 8 |
| β-strand | 374-375 | 2 | 8 |
| β-strand | 381-389 | 9 | 8 |
| α-helix | 394-395 | 2 | |
| β-strand | 396-401 | 6 | 9 |
| β-strand | 405-410 | 6 | 9 |
| β-strand | 415-419 | 5 | 9 |
| β-strand | 435-440 | 6 | 9 |
| β-strand | 449-456 | 8 | 1 |
| β-strand | 460-467 | 8 | 1 |
| α-helix | 468-469 | 2 | |
| α-helix | 472-480 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 89-96 | 8 | |
| α-helix | 101-115 | 15 | |
| α-helix | 123-128 | 6 | |
| α-helix | 132-137 | 6 | |
| α-helix | 145-159 | 15 | |
| α-helix | 163-171 | 9 | |
| α-helix | 175-184 | 10 | |
| α-helix | 187-203 | 17 | |
| α-helix | 205-213 | 9 | |
| α-helix | 217-222 | 6 | |
| α-helix | 223-225 | 3 | |
| α-helix | 229-242 | 14 | |
| α-helix | 252-255 | 4 | |
| α-helix | 256-258 | 3 | |
| α-helix | 259-265 | 7 | |
| α-helix | 271-284 | 14 | |
| α-helix | 289-297 | 9 | |
| α-helix | 301-306 | 6 | |
| α-helix | 313-326 | 14 | |
| α-helix | 331-339 | 9 | |
| α-helix | 342-349 | 8 | |
| α-helix | 355-368 | 14 | |
| α-helix | 373-381 | 9 | |
| α-helix | 385-394 | 10 | |
| α-helix | 397-411 | 15 | |
| α-helix | 412-414 | 3 | |
| α-helix | 419-426 | 8 | |
| α-helix | 430-439 | 10 | |
| α-helix | 442-462 | 21 | |
| α-helix | 475-479 | 5 | |
| α-helix | 483-487 | 5 | |
| α-helix | 495-508 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide exchange factor SRM1 | A | protein | 482 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P21827 (AlphaFold model) |
| Importin subunit alpha | B | protein | 542 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q02821 (AlphaFold model) |
>5T94_1 Guanine nucleotide exchange factor SRM1 (chains A) MVKRTVATNGDASGAHRAKKMSKTHASHIINAQEDYKHMYLSVQPLDIFCWGTGSMCELG LGPLAKNKEVKRPRLNPFLPRDEAKIISFAVGGMHTLALDEESNVWSWGCNDVGALGRDT SNAKEQLKDMDADDSSDDEDGDLNELESTPAKIPRESFPPLAEGHKVVQLAATDNMSCAL FSNGEVYAWGTFRCNEGILGFYQDKIKIQKTPWKVPTFSKYNIVQLAPGKDHILFLDEEG MVFAWGNGQQNQLGRKVMERFRLKTLDPRPFGLRHVKYIASGENHCFALTKDNKLVSWGL NQFGQCGVSEDVEDGALVTKPKRLALPDNVVIRSIAAGEHHSLILSQDGDLYSCGRLDMF EVGIPKDNLPEYTYKDVHGKARAVPLPTKLNNVPKFKSVAAGSHHSVAVAQNGIAYSWGF GETYAVGLGPFEDDTEVPTRIKNTATQDHNIILVGCGGQFSVSGGVKLSDEDAEKRADEM DD
>5T94_2 Importin subunit alpha (chains B) MDNGTDSSTSKFVPEYRRTNFKNKGRFSADELRRRRDTQQVELRKAKRDEALAKRRNFIP PTDGADSDEEDESSVSADQQFYSQLQQELPQMTQQLNSDDMQEQLSATVKFRQILSREHR PPIDVVIQAGVVPRLVEFMRENQPEMLQLEAAWALTNIASGTSAQTKVVVDADAVPLFIQ LLYTGSVEVKEQAIWALGNVAGDSTDYRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLS NLCRGKKPQPDWSVVSQALPTLAKLIYSMDTETLVDACWAISYLSDGPQEAIQAVIDVRI PKRLVELLSHESTLVQTPALRAVGNIVTGNDLQTQVVINAGVLPALRLLLSSPKENIKKE ACWTISNITAGNTEQIQAVIDANLIPPLVKLLEVAEYKTKKEACWAISNASSGGLQRPDI IRYLVSQGCIKPLCDLLEIADNRIIEVTLDALENILKMGEADKEARGLNINENADFIEKA GGMEKIFNCQQNENDKIYEKAYKIIETYFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFN FN
Three-dimensional context rather than NLS amino acid sequence determines importin alpha subtype specificity for RCC1. Sankhala, R.S., Lokareddy, R.K., Begum, S. et al. Nat Commun (2017) 8:979-979. DOI 10.1038/s41467-017-01057-7 · PubMed
Other PDB entries of the same protein (UniProt P21827 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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