The crystal structure of endosomal complex ESCRT-II (VPS22/VPS25/VPS36). Determined by X-ray diffraction at 3.6 Å resolution. Released 29 Sept 2004.
Explore 1W7P in 3D Show helices and sheets RCSB PDB PDBe
1W7P contains 44 α-helices and 28 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 | 26-49 | 24 | |
| α-helix | 50-56 | 7 | |
| α-helix | 58-71 | 14 | |
| α-helix | 75-78 | 4 | |
| α-helix | 86-105 | 20 | |
| β-strand | 113-115 | 3 | 1 |
| α-helix | 116-118 | 3 | |
| α-helix | 119-124 | 6 | |
| α-helix | 125-127 | 3 | |
| α-helix | 131-140 | 10 | |
| α-helix | 141-144 | 4 | |
| β-strand | 148-152 | 5 | 1 |
| β-strand | 155-159 | 5 | 1 |
| α-helix | 164-166 | 3 | |
| α-helix | 167-175 | 9 | |
| β-strand | 181-182 | 2 | 2 |
| α-helix | 184-190 | 7 | |
| α-helix | 196-207 | 12 | |
| β-strand | 212-214 | 3 | 2 |
| β-strand | 222-224 | 3 | 2 |
| α-helix | 227-230 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-9 | 4 | |
| α-helix | 11-14 | 4 | |
| α-helix | 20-40 | 21 | |
| β-strand | 45-47 | 3 | 3 |
| β-strand | 51-52 | 2 | 4 |
| β-strand | 73-74 | 2 | 4 |
| α-helix | 75-77 | 3 | |
| α-helix | 79-81 | 3 | |
| α-helix | 87-99 | 13 | |
| β-strand | 103-106 | 4 | 3 |
| α-helix | 116-118 | 3 | |
| β-strand | 120-123 | 4 | 3 |
| α-helix | 128-132 | 5 | |
| α-helix | 135-141 | 7 | |
| β-strand | 148-150 | 3 | 5 |
| α-helix | 151-155 | 5 | |
| α-helix | 170-177 | 8 | |
| α-helix | 178-180 | 3 | |
| β-strand | 188-190 | 3 | 5 |
| β-strand | 195-198 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| α-helix | 11-14 | 4 | |
| α-helix | 20-40 | 21 | |
| β-strand | 45-47 | 3 | 6 |
| β-strand | 51-52 | 2 | 7 |
| β-strand | 73-74 | 2 | 7 |
| α-helix | 87-99 | 13 | |
| β-strand | 103-106 | 4 | 6 |
| α-helix | 116-118 | 3 | |
| β-strand | 120-123 | 4 | 6 |
| α-helix | 128-142 | 15 | |
| β-strand | 148-149 | 2 | 8 |
| α-helix | 151-155 | 5 | |
| α-helix | 170-176 | 7 | |
| α-helix | 178-180 | 3 | |
| β-strand | 188-191 | 4 | 8 |
| β-strand | 194-198 | 5 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 404-421 | 18 | |
| β-strand | 434-436 | 3 | 9 |
| α-helix | 437-444 | 8 | |
| α-helix | 445-449 | 5 | |
| α-helix | 457-464 | 8 | |
| α-helix | 467-470 | 4 | |
| β-strand | 476-479 | 4 | 9 |
| β-strand | 485-488 | 4 | 9 |
| α-helix | 492-503 | 12 | |
| α-helix | 511-518 | 8 | |
| β-strand | 527 | 1 | 9 |
| α-helix | 529-541 | 13 | |
| β-strand | 545-550 | 6 | 10 |
| β-strand | 553-558 | 6 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| VPS22, YPL002C | A | protein | 233 | SACCHAROMYCES CEREVISIAE | Q12483 (AlphaFold model) |
| VPS25, YJR102C | B, C | protein | 202 | SACCHAROMYCES CEREVISIAE | P47142 (AlphaFold model) |
| VPS36P, YLR417W | D | protein | 566 | SACCHAROMYCES CEREVISIAE | Q06696 (AlphaFold model) |
>1W7P_1 VPS22, YPL002C (chains A) MKQFGLAAFDELKDGKYNDVNKTILEKQSVELRDQLMVFQERLVEFAKKHNSELQASPEF RSKFMHMCSSIGIDPLSLFDRDKHLFTVNDFYYEVCLKVIEICRQTKDMNGGVISFQELE KVHFRKLNVGLDDLEKSIDMLKSLECFEIFQIRGKKFLRSVPNELTSDQTKILEICSILG YSSISLLKANLGWEAVRSKSALDEMVANGLLWIDYQGGAEALYWDPSWITRQL
>1W7P_2 VPS25, YJR102C (chains B, C) MSALPPVYSFPPLYTRQPNSLTRRQQISTWIDIISQYCKTKKIWYMSVDGTVINDNELDS GSTDNDDSKKISKNLFNNEDIQRSVSQVFIDEIWSQMTKEGKCLPIDQSGRRSSNTTTTR YFILWKSLDSWASLILQWFEDSGKLNQVITLYELSEGDETVNWEFHRMPESLLYYCLKPL CDRNRATMLKDENDKVIAIKVV
>1W7P_3 VPS36P, YLR417W (chains D) MEYWHYVETTSSGQPLLREGEKDIFIDQSVGLYHGKSKILQRQRGRIFLTSQRIIYIDDA KPTQNSLGLELDDLAYVNYSSGFLTRSPRLILFFKDPSSKDELGKSAETASADVVSTWVC PICMVSNETQGEFTKDTLPTPICINCGVPADYELTKSSINCSNAIDPNANPQNQFGVNSE NICPACTFANHPQIGNCEICGHRLPNASKVRSKLNRLNFHDSRVHIELEKNSLARNKSSH SALSSSSSTGSSTEFVQLSFRKSDGVLFSQATERALENILTEKNKHIFNQNVVSVNGVDM RKGASSHEYNNEVPFIETKLSRIGISSLEKSRENQLLNNDILFNNALTDLNKLMSLATSI ERLYKNSNITMKTKTLNLQDESTVNEPKTRRPLLILDREKFLNKELFLDEIAREIYEFTL SEFKDLNSDTNYMIITLVDLYAMYNKSMRIGTGLISPMEMREACERFEHLGLNELKLVKV NKRILCVTSEKFDVVKEKLVDLIGDNPGSDLLRLTQILSSNNSKSNWTLGILMEVLQNCV DEGDLLIDKQLSGIYYYKNSYWPSHI
Escrt-II, an Endosome-Associated Complex Required for Protein Sorting: Crystal Structure and Interactions with Escrt-III and Membranes. Teo, H., Perisic, O., Gonzalez, B. et al. Dev Cell (2004) 7:559. DOI 10.1016/J.DEVCEL.2004.09.003 · 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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