TREX2 M-region. Determined by X-ray diffraction at 2.3 Å resolution. Released 5 Apr 2017.
Explore 5UBP in 3D Show helices and sheets RCSB PDB PDBe
5UBP contains 68 α-helices and 12 β-strands across 3 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 | 81-83 | 3 | |
| β-strand | 85 | 1 | 1 |
| α-helix | 90-96 | 7 | |
| α-helix | 103-106 | 4 | |
| α-helix | 113-115 | 3 | |
| β-strand | 117 | 1 | 1 |
| α-helix | 118-119 | 2 | |
| α-helix | 120-122 | 3 | |
| α-helix | 126-127 | 2 | |
| β-strand | 128 | 1 | 2 |
| α-helix | 138-153 | 16 | |
| α-helix | 157-177 | 21 | |
| α-helix | 187-189 | 3 | |
| α-helix | 206-215 | 10 | |
| α-helix | 220-222 | 3 | |
| α-helix | 231-232 | 2 | |
| α-helix | 238-242 | 5 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-254 | 3 | |
| α-helix | 258-271 | 14 | |
| α-helix | 273-275 | 3 | |
| α-helix | 280-296 | 17 | |
| β-strand | 299 | 1 | 2 |
| α-helix | 302-325 | 24 | |
| α-helix | 331-354 | 24 | |
| α-helix | 362-372 | 11 | |
| α-helix | 377-384 | 8 | |
| α-helix | 388-391 | 4 | |
| α-helix | 394-406 | 13 | |
| α-helix | 416-418 | 3 | |
| α-helix | 426-433 | 8 | |
| α-helix | 440-446 | 7 | |
| α-helix | 447-449 | 3 | |
| α-helix | 450-464 | 15 | |
| α-helix | 469-471 | 3 | |
| β-strand | 472-473 | 2 | 3 |
| α-helix | 474-481 | 8 | |
| α-helix | 486-495 | 10 | |
| β-strand | 499-501 | 3 | 3 |
| β-strand | 505-507 | 3 | 3 |
| α-helix | 508-510 | 3 | |
| α-helix | 522-526 | 5 | |
| α-helix | 530-536 | 7 | |
| α-helix | 541-545 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-12 | 10 | |
| α-helix | 23-37 | 15 | |
| α-helix | 42-51 | 10 | |
| α-helix | 59-74 | 16 | |
| α-helix | 80-96 | 17 | |
| α-helix | 106-128 | 23 | |
| α-helix | 131-134 | 4 | |
| α-helix | 140-155 | 16 | |
| α-helix | 156-160 | 5 | |
| α-helix | 170-173 | 4 | |
| α-helix | 175-188 | 14 | |
| α-helix | 192-194 | 3 | |
| α-helix | 195-205 | 11 | |
| α-helix | 211-213 | 3 | |
| α-helix | 216-232 | 17 | |
| α-helix | 236-251 | 16 | |
| α-helix | 258-277 | 20 | |
| β-strand | 282 | 1 | 4 |
| α-helix | 285-290 | 6 | |
| α-helix | 293-308 | 16 | |
| α-helix | 311-320 | 10 | |
| α-helix | 322-327 | 6 | |
| α-helix | 331-351 | 21 | |
| α-helix | 352-357 | 6 | |
| β-strand | 362-364 | 3 | 5 |
| α-helix | 365-376 | 12 | |
| α-helix | 400-409 | 10 | |
| β-strand | 416-418 | 3 | 5 |
| β-strand | 423-425 | 3 | 5 |
| α-helix | 432-435 | 4 | |
| α-helix | 439-446 | 8 | |
| α-helix | 448-450 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-31 | 4 | |
| α-helix | 35-37 | 3 | |
| β-strand | 60 | 1 | 4 |
| α-helix | 72-87 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Leucine permease transcriptional regulator | A | protein | 482 | Saccharomyces cerevisiae RM11-1a | B3LGC5 |
| Nuclear mRNA export protein THP1 | B | protein | 455 | Saccharomyces cerevisiae S288c | Q08231 (AlphaFold model) |
| 26S proteasome complex subunit SEM1 | C | protein | 89 | Saccharomyces cerevisiae S288c | O94742 (AlphaFold model) |
>5UBP_1 Leucine permease transcriptional regulator (chains A) SGSPSYTENKPDKKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHKARELPRFLINQEPQ LEKRAFVQDPWDKANQEKMISLEESIDDLNELYETLKKMRNTERSIMEEKGLVDKADSAK DLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRTKALKVFARPAAAAA PPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDFTYQNYSGPEAVDCN ERIVRIHLLILHIMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRSSGGTCPNEAEFRAY ALLSKIRDPQYDENIQRLPKHIFQDKLVQMALCFRRVISNSAYTERGFVKTENCLNFYAR FFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPFIYLENMLLFNNRQE IIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLERRLQKTTYKGLINGG ED
>5UBP_2 Nuclear mRNA export protein THP1 (chains B) MDMANQLLDELAHGNFSHLTLNLSQNGREIAILQKQLTGFDDKQLETFVEQHPAMPNDTR FKIMCTSFLNYARDVDPWSAWSSSDLIFEFYQCLINCLINDNAPHIEMLIPVATRETEFI INLAGKLDSFHLQLHTRSHQFLSHISSILSRLFNSIKPPRGNASSTNIPGKQRILLYLVN KLNNIYFRIESPQLCSNIFKNFQPKSMLAHFNEYQLDQQIEYRYLLGRYYLLNSQVHNAF VQFNEAFQSLLNLPLTNQAITRNGTRILNYMIPTGLILGKMVKWGPLRPFLSQETIDNWS VLYKHVRYGNIQGVSLWLRQNERHLCARQLLIVLLEKLPMVTYRNLIKTVIKSWTTEWGQ NKLPYSLIERVLQLSIGPTFEDPGAQEITIYNGIHSPKNVENVLVTLINLGLLRANCFPQ LQLCVVKKTTMIQEIVPPVNERITKMFPAHSHVLW
>5UBP_3 26S proteasome complex subunit SEM1 (chains C) MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIW EENWDDVEVDDDFTNELKAELDRYKRENQ
Structure of the Sac3 RNA-binding M-region in the Saccharomyces cerevisiae TREX-2 complex. Gordon, J.M.B., Aibara, S., Stewart, M. Nucleic Acids Res (2017) 45:5577-5585. DOI 10.1093/nar/gkx158 · PubMed
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