Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal sequence of INM protein Heh2. Determined by X-ray diffraction at 2.5 Å resolution. Released 26 Aug 2015.
Explore 4PVZ in 3D Show helices and sheets RCSB PDB PDBe
4PVZ contains 71 α-helices and 0 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 | 89-96 | 8 | |
| α-helix | 101-115 | 15 | |
| α-helix | 123-128 | 6 | |
| α-helix | 132-137 | 6 | |
| α-helix | 145-158 | 14 | |
| α-helix | 163-171 | 9 | |
| α-helix | 174-184 | 11 | |
| 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 | 300-307 | 8 | |
| 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 | 430-439 | 10 | |
| 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 | 89-96 | 8 | |
| α-helix | 101-114 | 14 | |
| α-helix | 123-128 | 6 | |
| α-helix | 132-137 | 6 | |
| α-helix | 145-158 | 14 | |
| α-helix | 163-171 | 9 | |
| α-helix | 174-184 | 11 | |
| 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 | 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 | 430-439 | 10 | |
| 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 | 113-118 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 105-108 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit alpha | A, B | protein | 422 | Saccharomyces cerevisiae S288c | Q02821 (AlphaFold model) |
| Inner nuclear membrane protein HEH2 | C, D | protein | 43 | Saccharomyces cerevisiae S288c | Q03281 (AlphaFold model) |
>4PVZ_1 Importin subunit alpha (chains A, B) ELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEML QLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDY RDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIY SMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIV TGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPP LVKLLEVAEYKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEV TLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIET YF
>4PVZ_2 Inner nuclear membrane protein HEH2 (chains C, D) GPLGSTNKRKREQISTDNEAKMQIQEEKSPKKKRKKRSSKANK
Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2. Lokareddy, R.K., Hapsari, R.A., van Rheenen, M. et al. Structure (2015) 23:1305-1316. DOI 10.1016/j.str.2015.04.017 · 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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