Cryo-EM structure of Karyopherin-beta2 bound to HNRNPH2 PY-NLS. Determined by electron microscopy at 3.17 Å resolution. Released 14 Jun 2023.
Explore 8SGH in 3D Show helices and sheets RCSB PDB PDBe
8SGH contains 71 α-helices and 0 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 | 17-29 | 13 | |
| α-helix | 35-48 | 14 | |
| α-helix | 54-63 | 10 | |
| α-helix | 70-87 | 18 | |
| α-helix | 88-90 | 3 | |
| α-helix | 93-105 | 13 | |
| α-helix | 112-128 | 17 | |
| α-helix | 131-133 | 3 | |
| α-helix | 137-145 | 9 | |
| α-helix | 150-166 | 17 | |
| α-helix | 168-172 | 5 | |
| α-helix | 180-189 | 10 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-207 | 12 | |
| α-helix | 215-218 | 4 | |
| α-helix | 221-230 | 10 | |
| α-helix | 237-253 | 17 | |
| α-helix | 255-258 | 4 | |
| α-helix | 259-261 | 3 | |
| α-helix | 262-273 | 12 | |
| α-helix | 278-293 | 16 | |
| α-helix | 297-300 | 4 | |
| α-helix | 302-304 | 3 | |
| α-helix | 305-315 | 11 | |
| α-helix | 318-319 | 2 | |
| α-helix | 320-326 | 7 | |
| α-helix | 372-379 | 8 | |
| α-helix | 383-398 | 16 | |
| α-helix | 399-402 | 4 | |
| α-helix | 403-413 | 11 | |
| α-helix | 419-431 | 13 | |
| α-helix | 433-440 | 8 | |
| α-helix | 441-443 | 3 | |
| α-helix | 444-454 | 11 | |
| α-helix | 460-472 | 13 | |
| α-helix | 474-479 | 6 | |
| α-helix | 482-486 | 5 | |
| α-helix | 487-497 | 11 | |
| α-helix | 502-519 | 18 | |
| α-helix | 520-526 | 7 | |
| α-helix | 527-540 | 14 | |
| α-helix | 543-560 | 18 | |
| α-helix | 561-564 | 4 | |
| α-helix | 567-583 | 17 | |
| α-helix | 591-605 | 15 | |
| α-helix | 606-612 | 7 | |
| α-helix | 613-636 | 24 | |
| α-helix | 642-644 | 3 | |
| α-helix | 646-663 | 18 | |
| α-helix | 664-667 | 4 | |
| α-helix | 668-671 | 4 | |
| α-helix | 676-685 | 10 | |
| α-helix | 689-704 | 16 | |
| α-helix | 707-710 | 4 | |
| α-helix | 711-713 | 3 | |
| α-helix | 714-725 | 12 | |
| α-helix | 730-747 | 18 | |
| α-helix | 748-751 | 4 | |
| α-helix | 754-766 | 13 | |
| α-helix | 773-789 | 17 | |
| α-helix | 791-794 | 4 | |
| α-helix | 795-797 | 3 | |
| α-helix | 798-809 | 12 | |
| α-helix | 816-831 | 16 | |
| α-helix | 834-839 | 6 | |
| α-helix | 840-848 | 9 | |
| α-helix | 855-868 | 14 | |
| α-helix | 876-881 | 6 | |
| α-helix | 886-894 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 205-207 | 3 | |
| α-helix | 211-212 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A | protein | 894 | Homo sapiens | Q92973 (AlphaFold model) |
| Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed | B | protein | 126 | Homo sapiens | P55795 (AlphaFold model) |
>8SGH_1 Transportin-1 (chains A) GGSKMEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTK LKSEDEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITT IASKGELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMI PKFLQFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVC RALVMLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRH LPKLIPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEE EDDDDDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKES GILVLGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDT YLKPLMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHK NLLILYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATA LQSGFLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLG GNIEQLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTN LNPEFISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIG RLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFC DAVASWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
>8SGH_2 Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed (chains B) GGSNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGMTLPVDFQGRSTGEAFVQF ASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGY NSIGRG
A new Karyopherin-beta 2 binding PY-NLS epitope of HNRNPH2 linked to neurodevelopmental disorders. Gonzalez, A., Kim, H.J., Freibaum, B.D. et al. Structure (2023) 31:924-934.e4. DOI 10.1016/j.str.2023.05.010 · PubMed
Other PDB entries of the same protein (UniProt Q92973 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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