2QMR: Karyopherin beta2/transportin

Karyopherin beta2/transportin. Determined by X-ray diffraction at 3.0 Å resolution. Released 30 Oct 2007.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Homo sapiens
Chains
4
Atoms
25,774
Mol. weight
405.63 kDa
Released
30 Oct 2007

Explore 2QMR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 61 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix7-2115
α-helix28-3710
α-helix44-496
α-helix50-545
α-helix62-7817
α-helix85-9612
α-helix104-12017
α-helix129-1368
α-helix142-15716
α-helix172-18211
α-helix188-19912
α-helix207-2104
α-helix213-2219
α-helix229-24517
α-helix247-2504
α-helix251-2533
α-helix254-26512
α-helix270-28415
α-helix289-2935
α-helix294-2963
α-helix297-30711
α-helix310-3112
α-helix312-3176
α-helix375-39016
α-helix391-3944
α-helix395-40612
α-helix411-42313
α-helix429-4324
α-helix433-4353
α-helix436-44611
α-helix452-46312
α-helix466-4716
α-helix478-48811
α-helix494-51118
α-helix512-5187
α-helix519-53214
α-helix536-55217
α-helix553-5564
α-helix559-57315
α-helix583-59614
α-helix599-6046
α-helix605-62824
α-helix634-6363
α-helix639-65416
α-helix660-6645
α-helix668-67710
α-helix681-70222
α-helix703-7053
α-helix706-71510
α-helix722-73918
α-helix740-7467
α-helix747-75812
α-helix765-78117
α-helix783-7864
α-helix787-7893
α-helix790-80112
α-helix808-82316
α-helix826-8294
α-helix832-8398
α-helix847-87327
α-helix878-88811
Chain B: 64 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix33-375
α-helix44-529
α-helix62-687
α-helix70-789
α-helix87-9711
α-helix104-12017
α-helix123-1253
α-helix129-1368
α-helix142-15716
α-helix172-1754
α-helix176-1816
α-helix182-1843
α-helix188-19912
α-helix207-2104
α-helix213-22412
α-helix229-24416
α-helix247-2493
α-helix251-2533
α-helix254-26512
α-helix270-28415
α-helix289-2935
α-helix297-30711
α-helix310-3112
α-helix312-3187
α-helix375-38915
α-helix392-3943
α-helix395-40612
α-helix411-42313
α-helix429-4324
α-helix433-4353
α-helix436-44611
α-helix452-46413
α-helix466-4716
α-helix478-48811
α-helix494-51017
α-helix513-5186
α-helix519-53214
α-helix535-55218
α-helix553-5564
α-helix559-57315
α-helix583-59715
α-helix602-6043
α-helix605-62824
α-helix639-65517
α-helix660-6645
α-helix668-67710
α-helix681-69717
α-helix699-7024
α-helix703-7053
α-helix706-71510
α-helix722-73918
α-helix740-7467
α-helix748-75912
α-helix765-78117
α-helix783-7864
α-helix787-7893
α-helix790-80011
α-helix808-82316
α-helix826-8294
α-helix832-8387
α-helix839-8435
α-helix847-86418
α-helix866-8738
α-helix878-88710
Chain C: 64 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix8-1912
α-helix33-375
α-helix44-529
α-helix62-687
α-helix70-789
α-helix87-9711
α-helix104-12017
α-helix123-1253
α-helix129-1368
α-helix142-15716
α-helix172-1754
α-helix176-1816
α-helix182-1843
α-helix188-20215
α-helix207-2104
α-helix213-22412
α-helix229-24416
α-helix247-2493
α-helix251-2533
α-helix254-26512
α-helix270-28415
α-helix289-2935
α-helix297-30711
α-helix310-3112
α-helix312-3187
α-helix375-38915
α-helix392-3943
α-helix395-40612
α-helix411-42313
α-helix429-4324
α-helix433-4353
α-helix436-44611
α-helix452-46413
α-helix466-4716
α-helix478-48811
α-helix494-51017
α-helix513-5186
α-helix519-53214
α-helix535-55218
α-helix553-5564
α-helix559-57517
α-helix583-59614
α-helix602-62827
α-helix639-65517
α-helix660-6645
α-helix668-67710
α-helix681-69717
α-helix699-7024
α-helix703-7053
α-helix706-71510
α-helix722-73918
α-helix740-7467
α-helix748-75912
α-helix765-78117
α-helix783-7864
α-helix787-7893
α-helix790-80011
α-helix808-82316
α-helix826-8294
α-helix832-8387
α-helix839-8435
α-helix848-86417
α-helix866-8738
α-helix878-88710
Chain D: 60 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix8-2114
α-helix28-3710
α-helix44-496
α-helix50-545
α-helix62-7817
α-helix85-9612
α-helix104-12017
α-helix129-1368
α-helix142-15716
α-helix172-18211
α-helix188-19912
α-helix207-2104
α-helix213-2219
α-helix229-24517
α-helix247-2504
α-helix251-2533
α-helix254-26512
α-helix270-28415
α-helix289-2935
α-helix297-30711
α-helix310-3112
α-helix312-3176
α-helix375-39016
α-helix391-3944
α-helix395-40612
α-helix411-42313
α-helix429-4324
α-helix433-4353
α-helix436-44611
α-helix452-46312
α-helix466-4716
α-helix478-48811
α-helix494-51118
α-helix512-5187
α-helix519-53214
α-helix536-55217
α-helix553-5564
α-helix559-57517
α-helix583-59614
α-helix599-6046
α-helix605-62824
α-helix634-6363
α-helix639-65416
α-helix660-6645
α-helix668-67710
α-helix681-70222
α-helix703-7053
α-helix706-71510
α-helix722-73918
α-helix740-7467
α-helix748-75811
α-helix765-78117
α-helix783-7864
α-helix787-7893
α-helix790-80112
α-helix808-82316
α-helix826-8294
α-helix832-8398
α-helix847-87327
α-helix878-88811

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transportin-1A, B, C, Dprotein890Homo sapiensQ92973 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2QMR_1 Transportin-1 (chains A, B, C, D)
MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE
DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK
GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL
QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV
MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL
IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDD
DDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILV
LGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKP
LMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLI
LYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSG
FLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIE
QLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPE
FISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGY
VCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVA
SWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV

Primary citation

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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