Structure of the ESCRT-II endosomal trafficking complex. Determined by X-ray diffraction at 3.6 Å resolution. Released 21 Sept 2004.
Explore 1U5T in 3D Show helices and sheets RCSB PDB PDBe
1U5T contains 34 α-helices and 24 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 | 23-49 | 27 | |
| α-helix | 58-71 | 14 | |
| α-helix | 75-78 | 4 | |
| α-helix | 83-85 | 3 | |
| α-helix | 88-106 | 19 | |
| β-strand | 114-115 | 2 | 1 |
| α-helix | 116-121 | 6 | |
| α-helix | 131-141 | 11 | |
| β-strand | 149-152 | 4 | 1 |
| β-strand | 155-158 | 4 | 1 |
| α-helix | 169-174 | 6 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-191 | 8 | |
| α-helix | 196-207 | 12 | |
| β-strand | 212-214 | 3 | 2 |
| β-strand | 222-224 | 3 | 2 |
| α-helix | 226-230 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 407-420 | 14 | |
| β-strand | 435-436 | 2 | 3 |
| α-helix | 439-446 | 8 | |
| α-helix | 457-464 | 8 | |
| α-helix | 468-470 | 3 | |
| β-strand | 476-480 | 5 | 3 |
| β-strand | 484-488 | 5 | 3 |
| α-helix | 493-505 | 13 | |
| β-strand | 509 | 1 | 4 |
| α-helix | 511-519 | 9 | |
| α-helix | 529-538 | 10 | |
| α-helix | 539-543 | 5 | |
| β-strand | 545-549 | 5 | 4 |
| β-strand | 554-558 | 5 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-9 | 4 | |
| α-helix | 11-14 | 4 | |
| α-helix | 20-38 | 19 | |
| β-strand | 45-46 | 2 | 5 |
| α-helix | 87-98 | 12 | |
| β-strand | 103-105 | 3 | 5 |
| β-strand | 121-123 | 3 | 5 |
| α-helix | 128-142 | 15 | |
| β-strand | 148-149 | 2 | 6 |
| α-helix | 151-154 | 4 | |
| α-helix | 170-177 | 8 | |
| β-strand | 187-188 | 2 | 6 |
| β-strand | 197-198 | 2 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-9 | 3 | |
| α-helix | 11-13 | 3 | |
| α-helix | 20-38 | 19 | |
| β-strand | 45-46 | 2 | 7 |
| α-helix | 87-100 | 14 | |
| β-strand | 105 | 1 | 7 |
| β-strand | 121-122 | 2 | 7 |
| α-helix | 129-132 | 4 | |
| β-strand | 149 | 1 | 8 |
| α-helix | 151-154 | 4 | |
| α-helix | 170-177 | 8 | |
| α-helix | 180-182 | 3 | |
| β-strand | 188 | 1 | 8 |
| β-strand | 197 | 1 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| appears to be functionally related to SNF7; Snf8p | A | protein | 233 | Saccharomyces cerevisiae | Q12483 (AlphaFold model) |
| Defective in vacuolar protein sorting; Vps36p | B | protein | 169 | Saccharomyces cerevisiae | Q06696 (AlphaFold model) |
| Hypothetical 23.6 kDa protein in YUH1-URA8 intergenic region | C, D | protein | 202 | Saccharomyces cerevisiae | P47142 (AlphaFold model) |
>1U5T_1 appears to be functionally related to SNF7; Snf8p (chains A) MKQFGLAAFDELKDGKYNDVNKTILEKQSVELRDQLMVFQERLVEFAKKHNSELQASPEF RSKFMHMCSSIGIDPLSLFDRDKHLFTVNDFYYEVCLKVIEICRQTKDMNGGVISFQELE KVHFRKLNVGLDDLEKSIDMLKSLECFEIFQIRGKKFLRSVPNELTSDQTKILEICSILG YSSISLLKANLGWEAVRSKSALDEMVANGLLWIDYQGGAEALYWDPSWITRQL
>1U5T_2 Defective in vacuolar protein sorting; Vps36p (chains B) LDREKFLNKELFLDEIAREIYEFTLSEFKDLNSDTNYMIITLVDLYAMYNKSMRIGTGLI SPMEMREACERFEHLGLNELKLVKVNKRILCVTSEKFDVVKEKLVDLIGDNPGSDLLRLT QILSSNNSKSNWTLGILMEVLQNCVDEGDLLIDKQLSGIYYYKNSYWPS
>1U5T_3 Hypothetical 23.6 kDa protein in YUH1-URA8 intergenic region (chains C, D) MSALPPVYSFPPLYTRQPNSLTRRQQISTWIDIISQYCKTKKIWYMSVDGTVINDNELDS GSTDNDDSKKISKNLFNNEDIQRSVSQVFIDEIWSQMTKEGKCLPIDQSGRRSSNTTTTR YFILWKSLDSWASLILQWFEDSGKLNQVITLYELSEGDETVNWEFHRMPESLLYYCLKPL CDRNRATMLKDENDKVIAIKVV
Structure of ESCRT-II endosomal trafficking complex. Hierro, A., Sun, J., Rusnak, A.S. et al. Nature (2004) 431:221-225. DOI 10.1038/nature02914 · PubMed
Other PDB entries of the same protein (UniProt Q12483 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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