Structure of S. cerevisiae Hrr25:Mam1 complex, form 2. Determined by X-ray diffraction at 2.89 Å resolution. Released 3 Aug 2016.
Explore 5CZO in 3D Show helices and sheets RCSB PDB PDBe
5CZO contains 60 α-helices and 30 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 |
|---|---|---|---|
| β-strand | 4-5 | 2 | 1 |
| β-strand | 9-16 | 8 | 1 |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 34-41 | 8 | 1 |
| α-helix | 49-58 | 10 | |
| α-helix | 66-67 | 2 | |
| β-strand | 68-74 | 7 | 1 |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 85-88 | 4 | 2 |
| α-helix | 89-95 | 7 | |
| α-helix | 102-120 | 19 | |
| β-strand | 124-125 | 2 | 3 |
| α-helix | 131-133 | 3 | |
| β-strand | 134-137 | 4 | 2 |
| α-helix | 139-141 | 3 | |
| β-strand | 145-147 | 3 | 2 |
| β-strand | 154-155 | 2 | 3 |
| β-strand | 157 | 1 | 4 |
| α-helix | 163 | 1 | |
| β-strand | 164 | 1 | 4 |
| α-helix | 165-167 | 3 | |
| α-helix | 182-185 | 4 | |
| α-helix | 188-190 | 3 | |
| α-helix | 192-208 | 17 | |
| α-helix | 221-234 | 14 | |
| α-helix | 237-240 | 4 | |
| α-helix | 246-256 | 11 | |
| α-helix | 262-264 | 3 | |
| α-helix | 266-279 | 14 | |
| α-helix | 289-309 | 21 | |
| α-helix | 327-343 | 17 | |
| α-helix | 361-372 | 12 | |
| α-helix | 380-387 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 6 |
| β-strand | 9-18 | 10 | 6 |
| β-strand | 21-28 | 8 | 6 |
| β-strand | 34-41 | 8 | 6 |
| α-helix | 49-58 | 10 | |
| β-strand | 68-74 | 7 | 6 |
| β-strand | 77-83 | 7 | 6 |
| β-strand | 85-88 | 4 | 7 |
| α-helix | 89-95 | 7 | |
| α-helix | 102-121 | 20 | |
| β-strand | 124-125 | 2 | 8 |
| α-helix | 131-133 | 3 | |
| β-strand | 134-137 | 4 | 7 |
| α-helix | 139-141 | 3 | |
| β-strand | 145-147 | 3 | 7 |
| β-strand | 154-155 | 2 | 8 |
| β-strand | 157 | 1 | 9 |
| α-helix | 163 | 1 | |
| β-strand | 164 | 1 | 9 |
| α-helix | 165-167 | 3 | |
| α-helix | 171-173 | 3 | |
| α-helix | 182-185 | 4 | |
| α-helix | 188-190 | 3 | |
| α-helix | 192-208 | 17 | |
| α-helix | 225-234 | 10 | |
| α-helix | 237-240 | 4 | |
| α-helix | 246-257 | 12 | |
| α-helix | 262-264 | 3 | |
| α-helix | 266-279 | 14 | |
| α-helix | 289-310 | 22 | |
| α-helix | 328-343 | 16 | |
| α-helix | 361-364 | 4 | |
| α-helix | 366-372 | 7 | |
| α-helix | 380-386 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 94-110 | 17 | |
| α-helix | 121-125 | 5 | |
| α-helix | 130-131 | 2 | |
| α-helix | 132-137 | 6 | |
| β-strand | 141 | 1 | 5 |
| α-helix | 148 | 1 | |
| α-helix | 149-158 | 10 | |
| α-helix | 159-161 | 3 | |
| α-helix | 180-181 | 2 | |
| α-helix | 184-186 | 3 | |
| β-strand | 188 | 1 | 5 |
| α-helix | 189-190 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 94-110 | 17 | |
| α-helix | 121-126 | 6 | |
| α-helix | 130-134 | 5 | |
| α-helix | 137-139 | 3 | |
| β-strand | 141 | 1 | 10 |
| α-helix | 148 | 1 | |
| α-helix | 149-158 | 10 | |
| α-helix | 159-161 | 3 | |
| α-helix | 184-186 | 3 | |
| β-strand | 188 | 1 | 10 |
| α-helix | 189-190 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Casein kinase I homolog HRR25 | A, B | protein | 395 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P29295 (AlphaFold model) |
| Monopolin complex subunit MAM1 | C, D | protein | 105 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40065 (AlphaFold model) |
>5CZO_1 Casein kinase I homolog HRR25 (chains A, B) AMDLRVGRKFRIGRKIGSGSFGDIYHGTNLISGEEVAIRLESIRSRHPQLDYESRVYRYL SGGVGIPFIRWFGREGEYNAMVIDLLGPSLEDLFNYCHRRFSFKTVIMLALQMFCRIQYI HGRSFIHRDIKPDNFLMGVGRRGSTVHVIDFGLSKKYRDFNTHRHIPYRENKSLTGTARY ASVNTHLGIEQSRRDDLESLGYVLIYFCKGSLPWQGLKATTKKQKYDRIMEKKLNVSVET LCSGLPLEFQEYMAYCKNLKFDEKPDYLFLARLFKDLSIKLEYHNDHLFDWTMLRYTKAM VEKQRDLLIEKGDLNANSNAASASNSTDNKSETFNKIKLLAMKKFPTHFHYYKNEDKHNP SPEEIKQQTILNNNAASSLPEELLNALDKGMENLR
>5CZO_2 Monopolin complex subunit MAM1 (chains C, D) EATECLTRSNLKKLQEKIFDRELNDIACDHCLCSTENRRDIKYSRLWFLFELEMSENWNE NLRLSCYNKYVYSAIDESWKMENILLKEQEKHYEYFPIGQLLIPN
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator. Ye, Q., Ur, S.N., Su, T.Y. et al. EMBO J (2016) 35:2139-2151. DOI 10.15252/embj.201694082 · PubMed
Other PDB entries of the same protein (UniProt P29295 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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