Crystal structure of the autoproteolytic domain from the nuclear pore complex component NUP145 from Saccharomyces cerevisiae. Determined by X-ray diffraction at 1.82 Å resolution. Released 22 Dec 2009.
Explore 3KEP in 3D Show helices and sheets RCSB PDB PDBe
3KEP contains 12 α-helices and 24 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 |
|---|---|---|---|
| β-strand | 461-464 | 4 | 1 |
| α-helix | 467-471 | 5 | |
| α-helix | 477-479 | 3 | |
| β-strand | 481 | 1 | 2 |
| β-strand | 485-488 | 4 | 1 |
| β-strand | 492-496 | 5 | 1 |
| β-strand | 500 | 1 | 2 |
| α-helix | 503-505 | 3 | |
| α-helix | 509-513 | 5 | |
| β-strand | 514 | 1 | 3 |
| β-strand | 518-521 | 4 | 3 |
| β-strand | 525-528 | 4 | 3 |
| α-helix | 535-537 | 3 | |
| β-strand | 546-550 | 5 | 1 |
| α-helix | 570-582 | 13 | |
| β-strand | 587-592 | 6 | 1 |
| β-strand | 597-602 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 461-464 | 4 | 4 |
| α-helix | 467-471 | 5 | |
| α-helix | 475-478 | 4 | |
| β-strand | 481 | 1 | 5 |
| β-strand | 485-488 | 4 | 4 |
| β-strand | 492-496 | 5 | 4 |
| β-strand | 500 | 1 | 5 |
| α-helix | 503-505 | 3 | |
| α-helix | 509-513 | 5 | |
| β-strand | 514 | 1 | 6 |
| β-strand | 518-521 | 4 | 6 |
| β-strand | 525-528 | 4 | 6 |
| α-helix | 535-537 | 3 | |
| β-strand | 546-550 | 5 | 4 |
| β-strand | 556 | 1 | 7 |
| β-strand | 563 | 1 | 7 |
| α-helix | 570-581 | 12 | |
| β-strand | 587-592 | 6 | 4 |
| β-strand | 597-602 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoporin NUP145 | A, B | protein | 174 | Saccharomyces cerevisiae | P49687 (AlphaFold model) |
>3KEP_1 Nucleoporin NUP145 (chains A, B) MSLNKQDGENTLQHEKSSSFGYWCSPSPEQLERLSLKQLAAVSNFVIGRRGYGCITFQHD VDLTAFTKSFREELFGKIVIFRSSKTVEVYPDEATKPMIGHGLNVPAIITLENVYPVDKK TKKPMKDTTKFAEFQVFDRKLRSMREMNYISYNPFGGTWTFKVNHFEGHHHHHH
Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145. Sampathkumar, P., Ozyurt, S.A., Do, J. et al. Proteins (2010) 78:1992-1998. DOI 10.1002/prot.22707 · PubMed
Other PDB entries of the same protein (UniProt P49687 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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