2Z5J: Free Transportin 1

Free Transportin 1. Determined by X-ray diffraction at 3.4 Å resolution. Released 23 Oct 2007.

Method
X-ray diffraction
Resolution
3.4 Å
Organism
Homo sapiens
Chains
1
Atoms
6,652
Mol. weight
101.41 kDa
Released
23 Oct 2007

Explore 2Z5J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Z5J contains 59 α-helices and 0 β-strands across 1 chain. 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: 59 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix9-2012
α-helix30-389
α-helix45-5410
α-helix62-7615
α-helix85-9612
α-helix104-12017
α-helix129-1379
α-helix143-15816
α-helix160-1634
α-helix172-1809
α-helix188-19912
α-helix207-2104
α-helix213-22311
α-helix229-24517
α-helix247-2504
α-helix251-2533
α-helix254-26411
α-helix270-28314
α-helix291-2944
α-helix297-30812
α-helix375-39016
α-helix391-3977
α-helix399-4046
α-helix413-42311
α-helix429-4324
α-helix436-44611
α-helix454-46310
α-helix466-4694
α-helix474-48714
α-helix494-51118
α-helix519-52911
α-helix530-5323
α-helix535-55218
α-helix553-5564
α-helix559-57416
α-helix583-59614
α-helix598-6047
α-helix605-62622
α-helix634-6352
α-helix639-65416
α-helix656-6594
α-helix660-6645
α-helix668-6758
α-helix681-70222
α-helix703-7053
α-helix706-71510
α-helix722-73918
α-helix740-7434
α-helix747-75913
α-helix765-78117
α-helix783-7864
α-helix787-7893
α-helix790-80112
α-helix808-82114
α-helix825-8273
α-helix832-8398
α-helix848-86417
α-helix870-8734
α-helix878-88710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transportin-1Aprotein890Homo sapiensQ92973 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2Z5J_1 Transportin-1 (chains A)
MEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSE
DEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASK
GELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFL
QFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALV
MLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKL
IPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDD
DDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILV
LGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKP
LMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLI
LYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSG
FLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIE
QLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPE
FISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGY
VCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVA
SWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV

Primary citation

Structural basis for substrate recognition and dissociation by human transportin 1. Imasaki, T., Shimizu, T., Hashimoto, H. et al. Mol Cell (2007) 28:57-67. DOI 10.1016/j.molcel.2007.08.006 · PubMed

Other PDB entries of the same protein (UniProt Q92973 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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