NUP84-NUP145C-SEC13 edge element of the NPC lattice. Determined by X-ray diffraction at 4.0 Å resolution. Released 27 Oct 2009.
Explore 3JRO in 3D Show helices and sheets RCSB PDB PDBe
3JRO contains 56 α-helices and 33 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 | 12-15 | 4 | 1 |
| β-strand | 24-28 | 5 | 1 |
| β-strand | 32-39 | 8 | 1 |
| β-strand | 42-49 | 8 | 1 |
| β-strand | 56-61 | 6 | 2 |
| α-helix | 62-63 | 2 | |
| β-strand | 69-74 | 6 | 2 |
| β-strand | 79-85 | 7 | 2 |
| β-strand | 88-95 | 8 | 2 |
| β-strand | 102-107 | 6 | 3 |
| α-helix | 108-109 | 2 | |
| α-helix | 110-112 | 3 | |
| β-strand | 115-120 | 6 | 3 |
| β-strand | 124-129 | 6 | 3 |
| β-strand | 139-142 | 4 | 3 |
| β-strand | 148-153 | 6 | 4 |
| α-helix | 154-156 | 3 | |
| α-helix | 168-170 | 3 | |
| β-strand | 173-177 | 5 | 4 |
| β-strand | 182-188 | 7 | 4 |
| β-strand | 193-200 | 8 | 4 |
| β-strand | 207-212 | 6 | 5 |
| β-strand | 220-226 | 7 | 5 |
| β-strand | 231-236 | 6 | 5 |
| β-strand | 244 | 1 | 5 |
| β-strand | 247 | 1 | 5 |
| β-strand | 260-262 | 3 | 6 |
| β-strand | 269-272 | 4 | 6 |
| β-strand | 278-279 | 2 | 6 |
| β-strand | 282 | 1 | 7 |
| β-strand | 290 | 1 | 7 |
| β-strand | 295 | 1 | 6 |
| α-helix | 1136-1141 | 6 | |
| β-strand | 1154 | 1 | 8 |
| β-strand | 1160 | 1 | 8 |
| β-strand | 1162-1163 | 2 | 9 |
| β-strand | 1171-1172 | 2 | 9 |
| α-helix | 1174-1176 | 3 | |
| α-helix | 1184-1186 | 3 | |
| α-helix | 1188-1195 | 8 | |
| β-strand | 1198-1202 | 5 | 10 |
| β-strand | 1209-1214 | 6 | 10 |
| α-helix | 1218-1222 | 5 | |
| α-helix | 1230-1241 | 12 | |
| α-helix | 1256-1282 | 27 | |
| α-helix | 1293-1298 | 6 | |
| α-helix | 1304-1313 | 10 | |
| α-helix | 1318-1322 | 5 | |
| α-helix | 1323-1325 | 3 | |
| α-helix | 1331-1345 | 15 | |
| α-helix | 1353-1360 | 8 | |
| α-helix | 1374-1377 | 4 | |
| α-helix | 1382-1391 | 10 | |
| α-helix | 1400-1408 | 9 | |
| α-helix | 1418-1427 | 10 | |
| α-helix | 1432-1440 | 9 | |
| α-helix | 1448-1457 | 10 | |
| α-helix | 1468-1484 | 17 | |
| α-helix | 1488-1496 | 9 | |
| α-helix | 1501-1514 | 14 | |
| α-helix | 1535-1552 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-48 | 13 | |
| α-helix | 51-54 | 4 | |
| α-helix | 60-64 | 5 | |
| α-helix | 66-81 | 16 | |
| α-helix | 105-107 | 3 | |
| α-helix | 114-127 | 14 | |
| α-helix | 145-150 | 6 | |
| α-helix | 153-156 | 4 | |
| α-helix | 160-165 | 6 | |
| α-helix | 171-189 | 19 | |
| α-helix | 193-200 | 8 | |
| α-helix | 206-211 | 6 | |
| α-helix | 213-217 | 5 | |
| α-helix | 225-227 | 3 | |
| α-helix | 240-251 | 12 | |
| α-helix | 258-268 | 11 | |
| α-helix | 274-276 | 3 | |
| α-helix | 283-303 | 21 | |
| α-helix | 310-312 | 3 | |
| α-helix | 324-330 | 7 | |
| α-helix | 331-333 | 3 | |
| α-helix | 342-352 | 11 | |
| α-helix | 355-368 | 14 | |
| α-helix | 383-385 | 3 | |
| α-helix | 390-392 | 3 | |
| α-helix | 395-398 | 4 | |
| α-helix | 400-403 | 4 | |
| α-helix | 409-421 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fusion Protein of Protein Transport Protein SEC13 and Nucleoporin NUP145 | A | protein | 753 | Saccharomyces cerevisiae | P49687 (AlphaFold model), Q04491 (AlphaFold model) |
| Nucleoporin NUP84 | C | protein | 426 | Saccharomyces cerevisiae | P52891 (AlphaFold model) |
>3JRO_1 Fusion Protein of Protein Transport Protein SEC13 and Nucleoporin NUP145 (chains A) MVVIANAHNELIHDAVLDYYGKRLATCSSDKTIKIFEVEGETHKLIDTLTGHEGPVWRVD WAHPKFGTILASCSYDGKVLIWKEENGRWSQIAVHAVHSASVNSVQWAPHEYGPLLLVAS SDGKVSVVEFKENGTTSPIIIDAHAIGVNSASWAPATIEEDGEHNGTKESRKFVTGGADN LVKIWKYNSDAQTYVLESTLEGHSDWVRDVAWSPTVLLRSYLASVSQDRTCIIWTQDNEQ GPWKKTLLKEEKFPDVLWRASWSLSGNVLALSGGDNKVTLWKENLEGKWEPAGEVHQGGG GSGGGGATSKEFDGPCQNEIDLLFSECNDEIDNAKLIMKERRFTASYTFAKFSTGSMLLT KDIVGKSGVSIKRLPTELQRKFLFDDVYLDKEIEKVTIEARKSNPYPQISESSLLFKDAL DYMEKTSSDYNLWKLSSILFDPVSYPYKTDNDQVKMALLKKERHCRLTSWIVSQIGPEIE EKIRNSSNEIEQIFLYLLLNDVVRASKLAIESKNGHLSVLISYLGSNDPRIRDLAELQLQ KWSTGGCSIDKNISKIYKLLSGSPFEGLFSLKELESEFSWLCLLNLTLCYGQIDEYSLES LVQSHLDKFSLPYDDPIGVIFQLYAANENTEKLYKEVRQRTNALDVQFCWYLIQTLRFNG TRVFSKETSDEATFAFAAQLEFAQLHGHSLFVSCFLNDDKAAEDTIKRLVMREITLLRAS TNDHILNRLKIPSQLIFNAQALKDRYEGNYLSE
>3JRO_2 Nucleoporin NUP84 (chains C) GSMELSPTYQTERFTKFSDTLKEFKIEQNNEQNPIDPFNIIREFRSAAGQLALDLANSGD ESNVISSKDWELEARFWHLVELLLVFRNADLDLDEMELHPYNSRGLFEKKLMQDNKQLYQ IWIVMVWLKENTYVMERPKNVPTSKWLNSITSGGLKSCDLDFPLRENTNVLDVKDKEEDH IFFKYIYELILAGAIDEALEEAKLSDNISICMILCGIQEYLNPVIDTQIANEFNTQQGIK KHSLWRRTVYSLSQQAGLDPYERAIYSYLSGAIPNQEVLQYSDWESDLHIHLNQILQTEI ENYLLENNQVGTDELILPLPSHALTVQEVLNRVASRHPSESEHPIRVLMASVILDSLPSV IHSSVEMLLDVVKGTEASNDIIDKPYLLRIVTHLAICLDIINPGSVEEVDKSKLITTYIS LLKLQG
Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice. Brohawn, S.G., Schwartz, T.U. Nat Struct Mol Biol (2009) 16:1173-1177. DOI 10.1038/nsmb.1713 · 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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