Crystal structure of the karyopherin Kap60p bound to the SUMO protease Ulp1p (150-340). Determined by X-ray diffraction at 2.5 Å resolution. Released 14 Dec 2016.
Explore 5H2W in 3D Show helices and sheets RCSB PDB PDBe
5H2W contains 69 α-helices and 0 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 | 90-96 | 7 | |
| 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 | 187-201 | 15 | |
| 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 | 301-307 | 7 | |
| α-helix | 313-326 | 14 | |
| α-helix | 331-339 | 9 | |
| α-helix | 342-349 | 8 | |
| α-helix | 355-368 | 14 | |
| α-helix | 373-381 | 9 | |
| α-helix | 385-394 | 10 | |
| α-helix | 397-411 | 15 | |
| α-helix | 412-414 | 3 | |
| α-helix | 419-426 | 8 | |
| α-helix | 430-436 | 7 | |
| α-helix | 442-464 | 23 | |
| α-helix | 472-479 | 8 | |
| α-helix | 482-488 | 7 | |
| α-helix | 489-491 | 3 | |
| α-helix | 495-508 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 90-96 | 7 | |
| α-helix | 101-115 | 15 | |
| α-helix | 123-127 | 5 | |
| α-helix | 132-137 | 6 | |
| α-helix | 145-159 | 15 | |
| α-helix | 163-171 | 9 | |
| α-helix | 175-184 | 10 | |
| α-helix | 187-201 | 15 | |
| α-helix | 205-213 | 9 | |
| α-helix | 217-222 | 6 | |
| α-helix | 223-225 | 3 | |
| α-helix | 229-242 | 14 | |
| 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 | 300-306 | 7 | |
| α-helix | 307-309 | 3 | |
| α-helix | 313-326 | 14 | |
| α-helix | 331-339 | 9 | |
| α-helix | 342-349 | 8 | |
| α-helix | 355-368 | 14 | |
| α-helix | 373-381 | 9 | |
| α-helix | 385-394 | 10 | |
| α-helix | 397-411 | 15 | |
| α-helix | 412-414 | 3 | |
| α-helix | 419-426 | 8 | |
| α-helix | 430-436 | 7 | |
| α-helix | 442-461 | 20 | |
| α-helix | 472-479 | 8 | |
| α-helix | 482-488 | 7 | |
| α-helix | 489-491 | 3 | |
| α-helix | 495-508 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha | A, C | protein | 423 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q02821 (AlphaFold model) |
| Ubiquitin-like-specific protease 1 | B, D | protein | 191 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q02724 (AlphaFold model) |
>5H2W_1 Importin subunit alpha (chains A, C) ELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEML QLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDY RDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIY SMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIV TGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPP LVKLLEVAEYKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEV TLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIET YFG
>5H2W_2 Ubiquitin-like-specific protease 1 (chains B, D) SSDTRKHKFDTSTWALPNKRRRIESEGVGTPSTSPISSLASQKSNCDSDNSITFSRDPFG WNKWKTSAIGSNSENNTSDQKNSYDRRQYGTAFIRKKKVAKQNINNTKLVSRAQSEEVTY LRQIFNGEYKVPKILKEERERQLKLMDMDKEKDTGLKKSIIDLTEKIKTILIENNKNRLQ TRNENDDDLVF
Structures of the Karyopherins Kap121p and Kap60p Bound to the Nuclear Pore-Targeting Domain of the SUMO Protease Ulp1p. Hirano, H., Kobayashi, J., Matsuura, Y. J Mol Biol (2017) 429:249-260. DOI 10.1016/j.jmb.2016.11.029 · 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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