Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5p. Determined by X-ray diffraction at 3.0 Å resolution. Released 20 Nov 2002.
Explore 1MQS in 3D Show helices and sheets RCSB PDB PDBe
1MQS contains 31 α-helices and 19 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 |
|---|---|---|---|
| α-helix | 14-26 | 13 | |
| α-helix | 43-49 | 7 | |
| β-strand | 54-58 | 5 | 1 |
| α-helix | 60-66 | 7 | |
| α-helix | 72-77 | 6 | |
| β-strand | 80-85 | 6 | 1 |
| β-strand | 93-102 | 10 | 1 |
| α-helix | 106-118 | 13 | |
| β-strand | 121-128 | 8 | 1 |
| α-helix | 134-145 | 12 | |
| α-helix | 150-152 | 3 | |
| β-strand | 153-158 | 6 | 1 |
| β-strand | 164-165 | 2 | 2 |
| β-strand | 170-172 | 3 | 2 |
| α-helix | 178-183 | 6 | |
| α-helix | 191-210 | 20 | |
| α-helix | 214 | 1 | |
| β-strand | 215-218 | 4 | 2 |
| α-helix | 223-240 | 18 | |
| β-strand | 260-265 | 6 | 2 |
| α-helix | 266-268 | 3 | |
| α-helix | 271-274 | 4 | |
| β-strand | 279 | 1 | 3 |
| α-helix | 280-287 | 8 | |
| β-strand | 295-297 | 3 | 4 |
| β-strand | 317-319 | 3 | 4 |
| α-helix | 328-331 | 4 | |
| β-strand | 335 | 1 | 3 |
| α-helix | 336-360 | 25 | |
| α-helix | 388-412 | 25 | |
| α-helix | 417-422 | 6 | |
| α-helix | 429-438 | 10 | |
| α-helix | 447-460 | 14 | |
| α-helix | 467-478 | 12 | |
| α-helix | 486-503 | 18 | |
| α-helix | 529-533 | 5 | |
| α-helix | 543-548 | 6 | |
| α-helix | 554-556 | 3 | |
| α-helix | 557-566 | 10 | |
| α-helix | 573-579 | 7 | |
| β-strand | 583-585 | 3 | 2 |
| β-strand | 605-611 | 7 | 2 |
| β-strand | 614 | 1 | 5 |
| α-helix | 616-626 | 11 | |
| β-strand | 635-640 | 6 | 2 |
| β-strand | 643 | 1 | 5 |
| α-helix | 646-659 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-4 | 5 | |
| β-strand | 5 | 1 | 1 |
| α-helix | 7-20 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sly1 Protein | A | protein | 671 | Saccharomyces cerevisiae | P22213 (AlphaFold model) |
| Integral Membrane Protein SED5 | B | protein | 50 | Saccharomyces cerevisiae | Q01590 (AlphaFold model) |
>1MQS_1 Sly1 Protein (chains A) GKSASMAVEEIASRKDISLRDMQISAILKMLFLNKDLNNNDNITTITDDIFNQQEIIWKV LILDIKSTATISSVLRVNDLLKAGITVHSLIKQDRSPLPDVPAIYFVSPTKENIDIIVND LKSDKYSEFYINFTSSLPRNLLEDLAQQVSITGKSDKIKQVYDQYLDFIVTEPELFSLEI SNAYLTLNDPKTTEEEITGLCANIADGLFNTVLTINSIPIIRAAKGGPAEIIAEKLGTKL RDFVINTNSSSTSTLQGNDSLERGVLIILDRNIDFASMFSHSWIYQCMVFDIFKLSRNTV TIPLESKENGTDNTTAKPLATKKYDIEPNDFFWMENSHLPFPEAAENVEAALNTYKEEAA EITRKTGVTNISDLDPNSNNDTVQIQEVVKKLPELTAKKNTIDTHMNIFAALLSQLESKS LDTFFEVEQDPGSTKTRSRFLDILKDGKTNNLEDKLRSFIVLYLTSTTGLPKDFVQNVEN YFKENDYDINALKYVYKLREFMQLSNMSLQNKSLEDGSDSAFKPSNLTLSGIYGLTEGKL QGGVGSLISGIKKLLPEKKTIPITNVVDAIMDPLNSSQKNLETTDSYLYIDPKITRGSHT RKPKRQSYNKSLVFVVGGGNYLEYQNLQEWAHSQLHNPKKVMYGSTAITTPAEFLNEISR LGASNSSNNDA
>1MQS_2 Integral Membrane Protein SED5 (chains B) GAMAGMNIKDRTSEFQQSVLSYKKRNKNFREQQRERLQEKESENFANNTT
Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p. Bracher, A., Weissenhorn, W. EMBO J (2002) 21:6114-6124. DOI 10.1093/emboj/cdf608 · PubMed
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