Karyopherin beta2/transportin. Determined by X-ray diffraction at 3.0 Å resolution. Released 30 Oct 2007.
Explore 2QMR in 3D Show helices and sheets RCSB PDB PDBe
2QMR contains 249 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 7-21 | 15 | |
| α-helix | 28-37 | 10 | |
| α-helix | 44-49 | 6 | |
| α-helix | 50-54 | 5 | |
| α-helix | 62-78 | 17 | |
| α-helix | 85-96 | 12 | |
| α-helix | 104-120 | 17 | |
| α-helix | 129-136 | 8 | |
| α-helix | 142-157 | 16 | |
| α-helix | 172-182 | 11 | |
| α-helix | 188-199 | 12 | |
| α-helix | 207-210 | 4 | |
| α-helix | 213-221 | 9 | |
| α-helix | 229-245 | 17 | |
| α-helix | 247-250 | 4 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-284 | 15 | |
| α-helix | 289-293 | 5 | |
| α-helix | 294-296 | 3 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-317 | 6 | |
| α-helix | 375-390 | 16 | |
| α-helix | 391-394 | 4 | |
| α-helix | 395-406 | 12 | |
| α-helix | 411-423 | 13 | |
| α-helix | 429-432 | 4 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-463 | 12 | |
| α-helix | 466-471 | 6 | |
| α-helix | 478-488 | 11 | |
| α-helix | 494-511 | 18 | |
| α-helix | 512-518 | 7 | |
| α-helix | 519-532 | 14 | |
| α-helix | 536-552 | 17 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-573 | 15 | |
| α-helix | 583-596 | 14 | |
| α-helix | 599-604 | 6 | |
| α-helix | 605-628 | 24 | |
| α-helix | 634-636 | 3 | |
| α-helix | 639-654 | 16 | |
| α-helix | 660-664 | 5 | |
| α-helix | 668-677 | 10 | |
| α-helix | 681-702 | 22 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-746 | 7 | |
| α-helix | 747-758 | 12 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-801 | 12 | |
| α-helix | 808-823 | 16 | |
| α-helix | 826-829 | 4 | |
| α-helix | 832-839 | 8 | |
| α-helix | 847-873 | 27 | |
| α-helix | 878-888 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-37 | 5 | |
| α-helix | 44-52 | 9 | |
| α-helix | 62-68 | 7 | |
| α-helix | 70-78 | 9 | |
| α-helix | 87-97 | 11 | |
| α-helix | 104-120 | 17 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-136 | 8 | |
| α-helix | 142-157 | 16 | |
| α-helix | 172-175 | 4 | |
| α-helix | 176-181 | 6 | |
| α-helix | 182-184 | 3 | |
| α-helix | 188-199 | 12 | |
| α-helix | 207-210 | 4 | |
| α-helix | 213-224 | 12 | |
| α-helix | 229-244 | 16 | |
| α-helix | 247-249 | 3 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-284 | 15 | |
| α-helix | 289-293 | 5 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-318 | 7 | |
| α-helix | 375-389 | 15 | |
| α-helix | 392-394 | 3 | |
| α-helix | 395-406 | 12 | |
| α-helix | 411-423 | 13 | |
| α-helix | 429-432 | 4 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-464 | 13 | |
| α-helix | 466-471 | 6 | |
| α-helix | 478-488 | 11 | |
| α-helix | 494-510 | 17 | |
| α-helix | 513-518 | 6 | |
| α-helix | 519-532 | 14 | |
| α-helix | 535-552 | 18 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-573 | 15 | |
| α-helix | 583-597 | 15 | |
| α-helix | 602-604 | 3 | |
| α-helix | 605-628 | 24 | |
| α-helix | 639-655 | 17 | |
| α-helix | 660-664 | 5 | |
| α-helix | 668-677 | 10 | |
| α-helix | 681-697 | 17 | |
| α-helix | 699-702 | 4 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-746 | 7 | |
| α-helix | 748-759 | 12 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-800 | 11 | |
| α-helix | 808-823 | 16 | |
| α-helix | 826-829 | 4 | |
| α-helix | 832-838 | 7 | |
| α-helix | 839-843 | 5 | |
| α-helix | 847-864 | 18 | |
| α-helix | 866-873 | 8 | |
| α-helix | 878-887 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-19 | 12 | |
| α-helix | 33-37 | 5 | |
| α-helix | 44-52 | 9 | |
| α-helix | 62-68 | 7 | |
| α-helix | 70-78 | 9 | |
| α-helix | 87-97 | 11 | |
| α-helix | 104-120 | 17 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-136 | 8 | |
| α-helix | 142-157 | 16 | |
| α-helix | 172-175 | 4 | |
| α-helix | 176-181 | 6 | |
| α-helix | 182-184 | 3 | |
| α-helix | 188-202 | 15 | |
| α-helix | 207-210 | 4 | |
| α-helix | 213-224 | 12 | |
| α-helix | 229-244 | 16 | |
| α-helix | 247-249 | 3 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-284 | 15 | |
| α-helix | 289-293 | 5 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-318 | 7 | |
| α-helix | 375-389 | 15 | |
| α-helix | 392-394 | 3 | |
| α-helix | 395-406 | 12 | |
| α-helix | 411-423 | 13 | |
| α-helix | 429-432 | 4 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-464 | 13 | |
| α-helix | 466-471 | 6 | |
| α-helix | 478-488 | 11 | |
| α-helix | 494-510 | 17 | |
| α-helix | 513-518 | 6 | |
| α-helix | 519-532 | 14 | |
| α-helix | 535-552 | 18 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-575 | 17 | |
| α-helix | 583-596 | 14 | |
| α-helix | 602-628 | 27 | |
| α-helix | 639-655 | 17 | |
| α-helix | 660-664 | 5 | |
| α-helix | 668-677 | 10 | |
| α-helix | 681-697 | 17 | |
| α-helix | 699-702 | 4 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-746 | 7 | |
| α-helix | 748-759 | 12 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-800 | 11 | |
| α-helix | 808-823 | 16 | |
| α-helix | 826-829 | 4 | |
| α-helix | 832-838 | 7 | |
| α-helix | 839-843 | 5 | |
| α-helix | 848-864 | 17 | |
| α-helix | 866-873 | 8 | |
| α-helix | 878-887 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-21 | 14 | |
| α-helix | 28-37 | 10 | |
| α-helix | 44-49 | 6 | |
| α-helix | 50-54 | 5 | |
| α-helix | 62-78 | 17 | |
| α-helix | 85-96 | 12 | |
| α-helix | 104-120 | 17 | |
| α-helix | 129-136 | 8 | |
| α-helix | 142-157 | 16 | |
| α-helix | 172-182 | 11 | |
| α-helix | 188-199 | 12 | |
| α-helix | 207-210 | 4 | |
| α-helix | 213-221 | 9 | |
| α-helix | 229-245 | 17 | |
| α-helix | 247-250 | 4 | |
| α-helix | 251-253 | 3 | |
| α-helix | 254-265 | 12 | |
| α-helix | 270-284 | 15 | |
| α-helix | 289-293 | 5 | |
| α-helix | 297-307 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-317 | 6 | |
| α-helix | 375-390 | 16 | |
| α-helix | 391-394 | 4 | |
| α-helix | 395-406 | 12 | |
| α-helix | 411-423 | 13 | |
| α-helix | 429-432 | 4 | |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| α-helix | 452-463 | 12 | |
| α-helix | 466-471 | 6 | |
| α-helix | 478-488 | 11 | |
| α-helix | 494-511 | 18 | |
| α-helix | 512-518 | 7 | |
| α-helix | 519-532 | 14 | |
| α-helix | 536-552 | 17 | |
| α-helix | 553-556 | 4 | |
| α-helix | 559-575 | 17 | |
| α-helix | 583-596 | 14 | |
| α-helix | 599-604 | 6 | |
| α-helix | 605-628 | 24 | |
| α-helix | 634-636 | 3 | |
| α-helix | 639-654 | 16 | |
| α-helix | 660-664 | 5 | |
| α-helix | 668-677 | 10 | |
| α-helix | 681-702 | 22 | |
| α-helix | 703-705 | 3 | |
| α-helix | 706-715 | 10 | |
| α-helix | 722-739 | 18 | |
| α-helix | 740-746 | 7 | |
| α-helix | 748-758 | 11 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-786 | 4 | |
| α-helix | 787-789 | 3 | |
| α-helix | 790-801 | 12 | |
| α-helix | 808-823 | 16 | |
| α-helix | 826-829 | 4 | |
| α-helix | 832-839 | 8 | |
| α-helix | 847-873 | 27 | |
| α-helix | 878-888 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transportin-1 | A, B, C, D | protein | 890 | Homo sapiens | Q92973 (AlphaFold model) |
>2QMR_1 Transportin-1 (chains A, B, C, D) MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDD DDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILV LGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKP LMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLI LYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSG FLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIE QLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPE FISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGY VCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVA SWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
Conformational heterogeneity of karyopherin beta2 is segmental. Cansizoglu, A.E., Chook, Y.M. Structure (2007) 15:1431-1441. DOI 10.1016/j.str.2007.09.009 · 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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