2C1T: Kap60p:Nup2 complex

Structure of the Kap60p:Nup2 complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 22 Nov 2005.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
SACCHAROMYCES CEREVISIAE
Chains
4
Atoms
7,273
Mol. weight
112.01 kDa
Released
22 Nov 2005

Explore 2C1T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C1T contains 72 α-helices and 5 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: 34 helices, 1 β-strand

ElementResiduesLengthSheet
α-helix89-957
α-helix101-11414
α-helix123-1286
α-helix132-1376
α-helix145-15915
α-helix163-1719
α-helix175-18410
α-helix187-20317
α-helix205-2139
α-helix217-2215
α-helix222-2254
α-helix229-24315
α-helix249-2502
α-helix252-2554
α-helix256-2583
α-helix259-2657
α-helix271-28515
α-helix289-2979
α-helix300-3078
α-helix313-32614
α-helix331-3399
α-helix342-3498
α-helix355-36612
α-helix373-3819
α-helix385-39410
α-helix397-41115
α-helix412-4143
α-helix418-4269
α-helix430-4367
α-helix442-46524
α-helix472-4798
α-helix482-4887
α-helix489-4913
β-strand49211
α-helix495-50814
Chain B: 33 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix89-968
α-helix101-11515
α-helix123-1286
α-helix132-1376
α-helix145-15915
α-helix163-1719
α-helix175-18410
α-helix187-20216
α-helix205-2139
α-helix217-2226
α-helix223-2253
α-helix229-24315
α-helix249-2502
α-helix252-2554
α-helix256-2583
α-helix259-2657
α-helix271-28414
α-helix289-2979
α-helix300-3078
α-helix313-32614
α-helix331-3399
α-helix342-3509
α-helix355-36915
α-helix373-3819
α-helix385-39410
α-helix397-41014
α-helix418-4269
α-helix430-4367
α-helix442-46524
α-helix472-4798
α-helix482-4887
α-helix489-4913
β-strand49212
α-helix495-50814
Chain C: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand3011
α-helix34-374
Chain D: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix28-292
β-strand3012
α-helix311
α-helix34-374
β-strand3813
α-helix40-434

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Importin alpha subunitA, Bprotein454SACCHAROMYCES CEREVISIAEQ02821 (AlphaFold model)
Nucleoporin NUP2C, Dprotein51SACCHAROMYCES CEREVISIAEP32499 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2C1T_1 IMPORTIN ALPHA SUBUNIT (chains A, B)
ELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEML
QLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDY
RDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIY
SMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIV
TGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPP
LVKLLEVAEDKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEV
TLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIET
YFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFNF
Sequence of entity 2 (C, D), FASTA
>2C1T_2 NUCLEOPORIN NUP2 (chains C, D)
MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFK

Primary citation

Nup50/Npap60 Function in Nuclear Import Complex Disassembly and Importin Recycling. Matsuura, Y., Stewart, M. EMBO J (2005) 24:3681. DOI 10.1038/SJ.EMBOJ.7600843 · PubMed

Other PDB entries of the same protein (UniProt Q02821 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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