Structure of the Kap60p:Nup2 complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 22 Nov 2005.
Explore 2C1T in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 89-95 | 7 | |
| α-helix | 101-114 | 14 | |
| α-helix | 123-128 | 6 | |
| α-helix | 132-137 | 6 | |
| α-helix | 145-159 | 15 | |
| α-helix | 163-171 | 9 | |
| α-helix | 175-184 | 10 | |
| α-helix | 187-203 | 17 | |
| α-helix | 205-213 | 9 | |
| α-helix | 217-221 | 5 | |
| α-helix | 222-225 | 4 | |
| α-helix | 229-243 | 15 | |
| α-helix | 249-250 | 2 | |
| α-helix | 252-255 | 4 | |
| α-helix | 256-258 | 3 | |
| α-helix | 259-265 | 7 | |
| α-helix | 271-285 | 15 | |
| α-helix | 289-297 | 9 | |
| α-helix | 300-307 | 8 | |
| α-helix | 313-326 | 14 | |
| α-helix | 331-339 | 9 | |
| α-helix | 342-349 | 8 | |
| α-helix | 355-366 | 12 | |
| α-helix | 373-381 | 9 | |
| α-helix | 385-394 | 10 | |
| α-helix | 397-411 | 15 | |
| α-helix | 412-414 | 3 | |
| α-helix | 418-426 | 9 | |
| α-helix | 430-436 | 7 | |
| α-helix | 442-465 | 24 | |
| α-helix | 472-479 | 8 | |
| α-helix | 482-488 | 7 | |
| α-helix | 489-491 | 3 | |
| β-strand | 492 | 1 | 1 |
| α-helix | 495-508 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 89-96 | 8 | |
| α-helix | 101-115 | 15 | |
| α-helix | 123-128 | 6 | |
| α-helix | 132-137 | 6 | |
| α-helix | 145-159 | 15 | |
| α-helix | 163-171 | 9 | |
| α-helix | 175-184 | 10 | |
| α-helix | 187-202 | 16 | |
| α-helix | 205-213 | 9 | |
| α-helix | 217-222 | 6 | |
| α-helix | 223-225 | 3 | |
| α-helix | 229-243 | 15 | |
| α-helix | 249-250 | 2 | |
| α-helix | 252-255 | 4 | |
| α-helix | 256-258 | 3 | |
| α-helix | 259-265 | 7 | |
| α-helix | 271-284 | 14 | |
| α-helix | 289-297 | 9 | |
| α-helix | 300-307 | 8 | |
| α-helix | 313-326 | 14 | |
| α-helix | 331-339 | 9 | |
| α-helix | 342-350 | 9 | |
| α-helix | 355-369 | 15 | |
| α-helix | 373-381 | 9 | |
| α-helix | 385-394 | 10 | |
| α-helix | 397-410 | 14 | |
| α-helix | 418-426 | 9 | |
| α-helix | 430-436 | 7 | |
| α-helix | 442-465 | 24 | |
| α-helix | 472-479 | 8 | |
| α-helix | 482-488 | 7 | |
| α-helix | 489-491 | 3 | |
| β-strand | 492 | 1 | 2 |
| α-helix | 495-508 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30 | 1 | 1 |
| α-helix | 34-37 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-29 | 2 | |
| β-strand | 30 | 1 | 2 |
| α-helix | 31 | 1 | |
| α-helix | 34-37 | 4 | |
| β-strand | 38 | 1 | 3 |
| α-helix | 40-43 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin alpha subunit | A, B | protein | 454 | SACCHAROMYCES CEREVISIAE | Q02821 (AlphaFold model) |
| Nucleoporin NUP2 | C, D | protein | 51 | SACCHAROMYCES CEREVISIAE | P32499 (AlphaFold model) |
>2C1T_1 IMPORTIN ALPHA SUBUNIT (chains A, B) ELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEML QLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDY RDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIY SMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIV TGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPP LVKLLEVAEDKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEV TLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIET YFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFNF
>2C1T_2 NUCLEOPORIN NUP2 (chains C, D) MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFK
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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