Nucleoporin Nup107/Nup133 interaction complex. Determined by X-ray diffraction at 2.53 Å resolution. Released 1 Jul 2008.
Explore 3CQC in 3D Show helices and sheets RCSB PDB PDBe
3CQC contains 25 α-helices and 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 668-680 | 13 | |
| α-helix | 682-684 | 3 | |
| α-helix | 685-701 | 17 | |
| α-helix | 705-714 | 10 | |
| α-helix | 719-723 | 5 | |
| α-helix | 738-767 | 30 | |
| α-helix | 770-776 | 7 | |
| α-helix | 782-821 | 40 | |
| α-helix | 837-838 | 2 | |
| α-helix | 840-867 | 28 | |
| α-helix | 871-875 | 5 | |
| α-helix | 877-882 | 6 | |
| α-helix | 888-891 | 4 | |
| α-helix | 894-912 | 19 | |
| β-strand | 916 | 1 | 1 |
| β-strand | 922 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 936-942 | 7 | |
| α-helix | 946-959 | 14 | |
| α-helix | 964-980 | 17 | |
| α-helix | 985-1006 | 22 | |
| α-helix | 1012-1015 | 4 | |
| α-helix | 1028-1034 | 7 | |
| α-helix | 1045-1051 | 7 | |
| α-helix | 1067-1079 | 13 | |
| α-helix | 1096-1102 | 7 | |
| α-helix | 1125-1128 | 4 | |
| α-helix | 1142-1155 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear pore complex protein Nup107 | A | protein | 270 | Homo sapiens | P57740 (AlphaFold model) |
| Nuclear pore complex protein Nup133 | B | protein | 227 | Homo sapiens | Q8WUM0 (AlphaFold model) |
>3CQC_1 Nuclear pore complex protein Nup107 (chains A) GSPALDTGTTEEDRLKIDVIDWLVFDPAQRAEALKQGNAIMRKFLASKKHEAAKEVFVKI PQDSIAEIYNQCEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNEWFKHMNSVPQKPA LIPQPTFTEKVAHEHKEKKYEMDFGIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVRED AKEDHERTHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKE ELRKLLQKLRESSLMLLDQGLDPLGYEIQL
>3CQC_2 Nuclear pore complex protein Nup133 (chains B) MASHMLSWLHEINSQELEKAHATLLGLANMETRYFAKKKTLLGLSKLAALASDFSEDMLQ EKIEEMAEQERFLLHQETLPEQLLAEKQLNLSAMPVLTAPQLIGLYICEENRRANEYDFK KALDLLEYIDEEEDININDLKLEILCKALQRDNWSSSDGKDDPIEVSKDSIFVKILQKLL KDGIQLSEYLPEVKDLLQADQLGSLKSNPYFEFVLKANYEYYVQGQI
Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex. Boehmer, T., Jeudy, S., Berke, I.C. et al. Mol Cell (2008) 30:721-731. DOI 10.1016/j.molcel.2008.04.022 · PubMed
Other PDB entries of the same protein (UniProt P57740 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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