Crystal structure of transportin-SR2, a karyopherin involved in human disease, in complex with Ran. Determined by X-ray diffraction at 2.9 Å resolution. Released 9 Apr 2014.
Explore 4OL0 in 3D Show helices and sheets RCSB PDB PDBe
4OL0 contains 69 α-helices and 9 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 |
|---|---|---|---|
| β-strand | 10-17 | 8 | 1 |
| α-helix | 23-30 | 8 | |
| β-strand | 45-54 | 10 | 1 |
| β-strand | 57-66 | 10 | 1 |
| α-helix | 70-72 | 3 | |
| α-helix | 77-79 | 3 | |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-140 | 3 | |
| β-strand | 144-148 | 5 | 1 |
| β-strand | 150 | 1 | 2 |
| β-strand | 155 | 1 | 2 |
| α-helix | 159-169 | 11 | |
| β-strand | 176 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-20 | 13 | |
| α-helix | 24-37 | 14 | |
| α-helix | 43-52 | 10 | |
| α-helix | 57-73 | 17 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-96 | 14 | |
| α-helix | 102-117 | 16 | |
| α-helix | 125-133 | 9 | |
| α-helix | 137-139 | 3 | |
| α-helix | 140-149 | 10 | |
| α-helix | 163-187 | 25 | |
| α-helix | 195-206 | 12 | |
| α-helix | 209-211 | 3 | |
| α-helix | 223-233 | 11 | |
| α-helix | 239-258 | 20 | |
| α-helix | 263-274 | 12 | |
| α-helix | 277-285 | 9 | |
| α-helix | 289-305 | 17 | |
| α-helix | 307-312 | 6 | |
| α-helix | 317-319 | 3 | |
| α-helix | 322-331 | 10 | |
| α-helix | 336-340 | 5 | |
| α-helix | 343-355 | 13 | |
| α-helix | 359-379 | 21 | |
| α-helix | 389-391 | 3 | |
| α-helix | 395-410 | 16 | |
| α-helix | 411-413 | 3 | |
| α-helix | 416-428 | 13 | |
| α-helix | 434-445 | 12 | |
| α-helix | 448-450 | 3 | |
| α-helix | 453-455 | 3 | |
| α-helix | 456-467 | 12 | |
| α-helix | 475-486 | 12 | |
| α-helix | 489-494 | 6 | |
| α-helix | 496-498 | 3 | |
| α-helix | 499-511 | 13 | |
| α-helix | 513-529 | 17 | |
| α-helix | 533-535 | 3 | |
| α-helix | 538-546 | 9 | |
| α-helix | 555-569 | 15 | |
| α-helix | 574-594 | 21 | |
| α-helix | 609-620 | 12 | |
| α-helix | 633-636 | 4 | |
| α-helix | 638-651 | 14 | |
| α-helix | 656-673 | 18 | |
| α-helix | 678-692 | 15 | |
| α-helix | 699-711 | 13 | |
| α-helix | 718-736 | 19 | |
| α-helix | 746-762 | 17 | |
| α-helix | 764-768 | 5 | |
| α-helix | 773-783 | 11 | |
| α-helix | 789-804 | 16 | |
| α-helix | 815-827 | 13 | |
| α-helix | 830-839 | 10 | |
| α-helix | 840-844 | 5 | |
| α-helix | 847-849 | 3 | |
| α-helix | 850-863 | 14 | |
| α-helix | 865-877 | 13 | |
| α-helix | 890-891 | 2 | |
| α-helix | 895-903 | 9 | |
| α-helix | 908-921 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding nuclear protein Ran | A | protein | 216 | Homo sapiens | P62826 (AlphaFold model) |
| Transportin-3 | B | protein | 921 | Homo sapiens | Q9Y5L0 (AlphaFold model) |
>4OL0_1 GTP-binding nuclear protein Ran (chains A) MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
>4OL0_2 Transportin-3 (chains B) GAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYF AAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSW KGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTVVS LLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSNLH EAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTEL CETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIH GIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECFAQ LYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYTSI ELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLL EIARSLDSFLLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSN GISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVERC CRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQGLL DMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIA STTLDHRDANCSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHTCC FCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHKQV TSAEECKQVCWALRDFTRLFR
Structure of transportin SR2, a karyopherin involved in human disease, in complex with Ran. Tsirkone, V.G., Beutels, K.G., Demeulemeester, J. et al. Acta Crystallogr Sect F Struct Biol Cryst Commun (2014) 70:723-729. DOI 10.1107/S2053230X14009492 · 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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