3IBV: Karyopherin cytosolic state

Karyopherin cytosolic state. Determined by X-ray diffraction at 3.1 Å resolution. Released 25 Aug 2009.

Method
X-ray diffraction
Resolution
3.1 Å
Organism
Schizosaccharomyces pombe
Chains
2
Atoms
12,876
Mol. weight
220.87 kDa
Ligands
CA
Released
25 Aug 2009

Explore 3IBV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3IBV contains 115 α-helices and 4 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.

Chain A: 57 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix2-1413
α-helix20-3516
α-helix39-468
α-helix55-7117
α-helix78-9417
α-helix103-11917
α-helix127-13812
α-helix141-15818
α-helix167-18317
α-helix185-20117
α-helix205-21814
α-helix224-2285
α-helix230-23910
α-helix243-25816
α-helix263-27917
α-helix289-31022
α-helix318-33013
α-helix332-3398
α-helix344-3485
α-helix351-36414
α-helix369-3713
α-helix372-38716
α-helix391-3922
α-helix406-42621
α-helix428-44619
α-helix451-46717
α-helix475-4773
β-strand47911
α-helix4851
β-strand48611
α-helix4871
α-helix488-49811
α-helix507-51913
α-helix521-5255
α-helix531-5388
α-helix552-56514
α-helix574-5807
α-helix583-5853
α-helix602-6076
α-helix611-62717
α-helix632-65423
α-helix663-67917
α-helix691-70818
α-helix713-72614
α-helix731-7344
α-helix738-74811
α-helix754-76714
α-helix773-79018
α-helix800-82021
α-helix825-8284
α-helix830-8334
α-helix836-84611
α-helix854-86815
α-helix879-89214
α-helix893-8953
α-helix908-93124
α-helix932-9365
α-helix946-9527
α-helix971-9744
Chain B: 58 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix2-1413
α-helix22-3514
α-helix39-468
α-helix55-7117
α-helix78-9316
α-helix102-11918
α-helix127-13812
α-helix141-15818
α-helix167-18317
α-helix185-20117
α-helix205-21814
α-helix224-2274
α-helix231-2388
α-helix239-2413
α-helix243-2453
α-helix246-25712
α-helix263-28018
α-helix289-31123
α-helix318-33013
α-helix332-3398
α-helix344-3485
α-helix351-36414
α-helix372-38716
α-helix391-3922
α-helix406-42621
α-helix428-44619
α-helix451-46818
α-helix475-4773
β-strand47912
α-helix4851
β-strand48612
α-helix4871
α-helix488-49811
α-helix500-5023
α-helix507-51913
α-helix521-5255
α-helix531-5388
α-helix551-56515
α-helix569-5713
α-helix574-5818
α-helix582-5843
α-helix602-6076
α-helix611-62717
α-helix632-65322
α-helix654-6563
α-helix663-67917
α-helix690-70819
α-helix714-72916
α-helix731-7344
α-helix738-74710
α-helix754-76714
α-helix773-79018
α-helix800-82122
α-helix836-84510
α-helix855-86814
α-helix879-89214
α-helix910-92112
α-helix930-9312
α-helix932-9365
α-helix945-95410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Exportin-TA, Bprotein980Schizosaccharomyces pombeO94258 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3IBV_1 Exportin-T (chains A, B)
GPMSAQDVENAVEAALDPSVGPIIKQQATDFIGSLRSSSTGWKICHEIFSEKTKYKPSTR
LICLQTLSEKVREWNNESNLLELQMIRDSVWSYIKELSFLDEPAYISNAVQHLLTLLFLQ
LYPSNWNDFFASLQGVIAASSQSEFSNFYLKVLLSIGDEIADSLVLKTDVQIQKDNLVKD
AIRANDMSDIVSFVYEMMLAYSNAKNYGTVGLCLQVYAQWVSWININLIVNEPCMNLLYS
FLQIEELRCAACETMTEIVNKKMKPLEKLNLLNILNLNLFFSKSQEQSTDPNFDEHVAKL
INAQGVELVAIKSDPSELSPELKENCSFQLYNLFPYLIRYLSDDYDETSTAVFPFLSDLL
VSLRKESSSKELSASLKEFLKSLLEAIIKKMKYDESQEWDDDPDSEEEAEFQEMRKKLKI
FQDTINSIDSSLFSSYMYSAITSSLSTAATLSPENSWQLIEFALYETYIFGEGLRGPDAF
FNEVDKSPTVLSQILALVTTSQVCRHPHPLVQLLYMEILVRYASFFDYESAAIPALIEYF
VGPRGIHNTNERVRPRAWYLFYRFVKSIKKQVVNYTESSLAMLGDLLNISVSPVTDMDAP
VPTLNSSIRNSDFNSQLYLFETVGVLISSGNLTPEEQALYCDSLINALIGKANAALSSDL
SALENIISVYCSLMAIGNFAKGFPARGSEEVAWLASFNKASDEIFLILDRMGFNEDIRGA
VRFTSGRIINVVGPDMLPKVPQLISILLNSIDMNELVDVLSFISQLIHIYKDNMMEITNR
MLPTLLMRIFSSLSAAPQGTDDAVKQNDLRKSYISFILQLLNKGFGSILFTEENQVYFDP
LINSILHFANLVGEPATQKSSIALVSKMVSLWGGKDGIAGFENFTLSLTPLCFEMPVNPN
FNTRDGQSLVVLGELAGLQKIILEKLGDIYKSYLVTVYFPTVNFPDVMASEYLQALSNLD
SRSFKQFFQKFIQALKSGNV

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa4

Primary citation

Structures of the tRNA export factor in the nuclear and cytosolic states. Cook, A.G., Fukuhara, N., Jinek, M. et al. Nature (2009) 461:60-65. DOI 10.1038/nature08394 · PubMed

Other PDB entries of the same protein (UniProt O94258 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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