4C0P: Unliganded Transportin 3

Unliganded Transportin 3. Determined by X-ray diffraction at 2.95 Å resolution. Released 22 Jan 2014.

Method
X-ray diffraction
Resolution
2.95 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
28,293
Mol. weight
417.74 kDa
Ligands
DTT
Released
22 Jan 2014

Explore 4C0P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C0P contains 250 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: 63 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-74
α-helix8-2013
α-helix24-3815
α-helix43-5311
α-helix57-7317
α-helix82-9716
α-helix102-11817
α-helix125-1339
α-helix134-1363
α-helix140-15314
α-helix164-17512
α-helix177-18812
α-helix198-21013
α-helix216-2205
α-helix223-23311
α-helix239-25517
α-helix263-27412
α-helix277-2859
α-helix289-30517
α-helix307-3126
α-helix317-3193
α-helix322-33211
α-helix336-3394
α-helix340-3423
α-helix343-35513
α-helix359-37921
α-helix381-3833
α-helix389-3913
α-helix395-41016
α-helix411-4133
α-helix416-42510
α-helix434-44714
α-helix458-46710
α-helix475-48612
α-helix489-4935
α-helix496-4983
α-helix499-51113
α-helix513-5153
α-helix516-52914
α-helix533-5353
α-helix538-5469
α-helix548-5503
α-helix555-56915
α-helix574-59421
α-helix609-62113
α-helix635-65117
α-helix656-67217
α-helix681-69414
α-helix699-71113
α-helix715-7173
α-helix718-73619
α-helix741-7444
α-helix746-76015
α-helix764-7696
α-helix773-78311
α-helix789-80315
α-helix804-8063
α-helix815-83925
α-helix840-8445
α-helix847-8493
α-helix850-87627
α-helix893-90311
α-helix908-91912
Chain B: 62 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-74
α-helix8-2013
α-helix24-3815
α-helix43-5311
α-helix57-7317
α-helix82-9716
α-helix102-11817
α-helix125-1339
α-helix134-1363
α-helix140-15314
α-helix164-17512
α-helix177-18812
α-helix198-21013
α-helix216-2205
α-helix223-23311
α-helix239-25517
α-helix263-27412
α-helix276-28510
α-helix289-30517
α-helix307-3126
α-helix317-3193
α-helix322-33211
α-helix336-3394
α-helix340-3423
α-helix343-35513
α-helix359-37921
α-helix381-3833
α-helix389-3913
α-helix395-41016
α-helix411-4133
α-helix416-42510
α-helix434-44714
α-helix458-46710
α-helix475-48612
α-helix489-4935
α-helix496-4983
α-helix499-51113
α-helix513-5153
α-helix516-52914
α-helix533-5353
α-helix538-5469
α-helix548-5503
α-helix555-57016
α-helix574-59421
α-helix609-62113
α-helix633-65119
α-helix656-67217
α-helix681-69414
α-helix699-71113
α-helix715-7173
α-helix718-73619
α-helix741-7444
α-helix746-76015
α-helix764-7696
α-helix773-78311
α-helix789-80315
α-helix804-8063
α-helix815-83925
α-helix840-8445
α-helix849-87628
α-helix893-90311
α-helix908-91912
Chain C: 63 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-74
α-helix8-2013
α-helix24-3815
α-helix43-5311
α-helix57-7317
α-helix82-9716
α-helix102-11817
α-helix125-1339
α-helix134-1363
α-helix140-15314
α-helix164-17512
α-helix177-18812
α-helix198-21013
α-helix216-2205
α-helix223-23311
α-helix239-25517
α-helix263-27412
α-helix277-2859
α-helix289-30517
α-helix307-3126
α-helix317-3193
α-helix322-33211
α-helix336-3394
α-helix340-3423
α-helix343-35513
α-helix359-37921
α-helix381-3833
α-helix389-3913
α-helix395-41016
α-helix411-4133
α-helix416-42510
α-helix434-44714
α-helix458-46710
α-helix475-48612
α-helix489-4935
α-helix496-4983
α-helix499-51113
α-helix513-5153
α-helix516-52914
α-helix533-5353
α-helix538-5469
α-helix548-5503
α-helix555-57016
α-helix574-59421
α-helix609-62113
α-helix635-65117
α-helix656-67217
α-helix681-69414
α-helix699-71113
α-helix715-7173
α-helix718-73619
α-helix741-7444
α-helix746-76015
α-helix764-7696
α-helix773-78311
α-helix789-80315
α-helix804-8063
α-helix815-83925
α-helix840-8445
α-helix847-8493
α-helix850-87627
α-helix893-90311
α-helix908-91912
Chain D: 62 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-74
α-helix8-2013
α-helix24-3815
α-helix43-5311
α-helix57-7317
α-helix82-9716
α-helix102-11817
α-helix125-1339
α-helix134-1363
α-helix140-15314
α-helix164-17512
α-helix177-18812
α-helix198-21013
α-helix216-2205
α-helix223-23311
α-helix239-25517
α-helix263-27412
α-helix276-28510
α-helix289-30517
α-helix307-3126
α-helix317-3193
α-helix322-33211
α-helix336-3394
α-helix340-3423
α-helix343-35513
α-helix359-37921
α-helix381-3833
α-helix389-3913
α-helix395-41016
α-helix411-4133
α-helix416-42510
α-helix434-44714
α-helix458-46710
α-helix475-48612
α-helix489-4935
α-helix496-4983
α-helix499-51113
α-helix513-5153
α-helix516-52914
α-helix533-5353
α-helix538-5469
α-helix548-5503
α-helix555-57016
α-helix574-59421
α-helix609-62113
α-helix635-65117
α-helix656-67217
α-helix681-69414
α-helix699-71113
α-helix715-73622
α-helix741-7444
α-helix746-76015
α-helix764-7696
α-helix773-78311
α-helix789-80315
α-helix804-8063
α-helix815-83925
α-helix840-8445
α-helix847-8493
α-helix850-87627
α-helix893-90311
α-helix908-91912

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transportin-3A, B, C, Dprotein923HOMO SAPIENSQ9Y5L0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4C0P_1 TRANSPORTIN-3 (chains A, B, C, D)
MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESC
YFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMP
SWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTV
VSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSN
LHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFT
ELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEV
IHGIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECF
AQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYT
SIELVGEMSEVVDRNPQFLDPVLGYLMKGLAEKPLASAAAKAIHNICSVCRDHMAQHFNG
LLEIARSLDSFLLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEP
SNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVE
RCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQG
LLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWA
IASTTLDHRDANCSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHT
CCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHK
QVTSAEECKQVCWALRDFTRLFR

Ligands and cofactors

IDNameFormulaCopies
DTT2,3-dihydroxy-1,4-dithiobutaneC4 H10 O2 S24

Primary citation

Structural Basis for Nuclear Import of Splicing Factors by Human Transportin 3. Maertens, G.N., Cook, N.J., Wang, W. et al. Proc Natl Acad Sci U S A (2014) 111:2728. DOI 10.1073/PNAS.1320755111 · PubMed

Other PDB entries of the same protein (UniProt Q9Y5L0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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