Kap95p Binding Induces the Switch Loops of RanGDP to adopt the GTP-bound Conformation: Implications for Nuclear Import Complex Assembly Dynamics. Determined by X-ray diffraction at 2.5 Å resolution. Released 21 Oct 2008.
Explore 3EA5 in 3D Show helices and sheets RCSB PDB PDBe
3EA5 contains 134 α-helices and 13 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 |
|---|---|---|---|
| β-strand | 10-17 | 8 | 1 |
| α-helix | 23-32 | 10 | |
| α-helix | 34-36 | 3 | |
| β-strand | 45-54 | 10 | 1 |
| β-strand | 57-66 | 10 | 1 |
| α-helix | 70-72 | 3 | |
| α-helix | 76-80 | 5 | |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 138-140 | 3 | |
| β-strand | 144-148 | 5 | 1 |
| α-helix | 159-169 | 11 | |
| β-strand | 176 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-35 | 17 | |
| α-helix | 37-48 | 12 | |
| α-helix | 55-66 | 12 | |
| α-helix | 74-87 | 14 | |
| α-helix | 90-104 | 15 | |
| α-helix | 109-126 | 18 | |
| α-helix | 127-129 | 3 | |
| α-helix | 135-142 | 8 | |
| α-helix | 149-165 | 17 | |
| α-helix | 180-187 | 8 | |
| α-helix | 195-208 | 14 | |
| 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 | 268-275 | 8 | |
| 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 | 383-394 | 12 | |
| 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 | 536-554 | 19 | |
| 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 | 615-629 | 15 | |
| α-helix | 630-633 | 4 | |
| α-helix | 634-649 | 16 | |
| α-helix | 654-670 | 17 | |
| 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 | 819-823 | 5 | |
| α-helix | 825-836 | 12 | |
| α-helix | 842-859 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-16 | 7 | 2 |
| α-helix | 23-32 | 10 | |
| β-strand | 45-55 | 11 | 2 |
| β-strand | 57-66 | 10 | 2 |
| α-helix | 70-72 | 3 | |
| α-helix | 76-80 | 5 | |
| β-strand | 85-91 | 7 | 2 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 2 |
| β-strand | 144-148 | 5 | 2 |
| α-helix | 159-169 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-35 | 17 | |
| α-helix | 37-48 | 12 | |
| α-helix | 55-66 | 12 | |
| α-helix | 74-87 | 14 | |
| α-helix | 90-104 | 15 | |
| α-helix | 109-129 | 21 | |
| α-helix | 135-142 | 8 | |
| α-helix | 149-163 | 15 | |
| α-helix | 180-187 | 8 | |
| α-helix | 195-207 | 13 | |
| α-helix | 213-216 | 4 | |
| α-helix | 219-232 | 14 | |
| α-helix | 238-255 | 18 | |
| α-helix | 256-258 | 3 | |
| α-helix | 260-262 | 3 | |
| α-helix | 263-267 | 5 | |
| α-helix | 268-275 | 8 | |
| 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 | 516-529 | 14 | |
| α-helix | 533-535 | 3 | |
| α-helix | 536-554 | 19 | |
| α-helix | 563-586 | 24 | |
| α-helix | 588-590 | 3 | |
| α-helix | 592-594 | 3 | |
| α-helix | 595-607 | 13 | |
| α-helix | 615-629 | 15 | |
| α-helix | 631-633 | 3 | |
| α-helix | 634-649 | 16 | |
| α-helix | 654-670 | 17 | |
| 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 | 819-823 | 5 | |
| α-helix | 825-835 | 11 | |
| α-helix | 842-859 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding nuclear protein Ran | A, C | protein | 216 | Homo sapiens | P62826 (AlphaFold model) |
| Importin subunit beta-1 | B, D | protein | 861 | Saccharomyces cerevisiae | Q06142 (AlphaFold model) |
>3EA5_1 GTP-binding nuclear protein Ran (chains A, C) MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP CLAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
>3EA5_2 Importin subunit beta-1 (chains B, D) MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRIL AALTLKNELVSKDSVKTQQFAQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIA AIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALGYMCESADPQSQALVSSSNNI LIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEV QAAAFGCLCKIMSKYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDI AYELAQFPQSPLQSYNFALSSIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQ NCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGPDKVQRTYYVHQALPSILNLM NDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINL VEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSA SISTFVMDKLGQTMSVDENQLTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMG LFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETFSPYLLKALNQVDSPVSITAV GFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPY LNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIF QFIAQVAEDPQLYSEDATSRAAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLF SQATKDTARWAREQQKRQLSL
Kap95p binding induces the switch loops of RanGDP to adopt the GTP-bound conformation: implications for nuclear import complex assembly dynamics. Forwood, J.K., Lonhienne, T.G., Marfori, M. et al. J Mol Biol (2008) 383:772-782. DOI 10.1016/j.jmb.2008.07.090 · PubMed
Other PDB entries of the same protein (UniProt P62826 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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