Structure of a complex between S. cerevisiae Csm1 and Mam1. Determined by X-ray diffraction at 3.05 Å resolution. Released 20 Jul 2016.
Explore 5KTB in 3D Show helices and sheets RCSB PDB PDBe
5KTB contains 14 α-helices and 10 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 | 21-82 | 62 | |
| β-strand | 84-91 | 8 | 1 |
| β-strand | 96-103 | 8 | 1 |
| β-strand | 115-122 | 8 | 1 |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 143-152 | 10 | |
| α-helix | 155-158 | 4 | |
| β-strand | 161-164 | 4 | 1 |
| α-helix | 166-179 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-82 | 66 | |
| β-strand | 84-91 | 8 | 2 |
| β-strand | 95-103 | 9 | 2 |
| β-strand | 115-123 | 9 | 2 |
| β-strand | 132-136 | 5 | 2 |
| α-helix | 143-152 | 10 | |
| α-helix | 155-158 | 4 | |
| β-strand | 161-163 | 3 | 2 |
| α-helix | 165-167 | 3 | |
| α-helix | 168-180 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 227-229 | 3 | |
| α-helix | 231-233 | 3 | |
| α-helix | 234-237 | 4 | |
| α-helix | 240-242 | 3 | |
| α-helix | 247-253 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monopolin complex subunit CSM1 | A, B | protein | 190 | Saccharomyces cerevisiae | P25651 (AlphaFold model) |
| Monopolin complex subunit MAM1 | C | protein | 70 | Saccharomyces cerevisiae | P40065 (AlphaFold model) |
>5KTB_1 Monopolin complex subunit CSM1 (chains A, B) MDPLTVYKNSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKEL KTQTSQQAENSEVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGGSSDDYSIMDYKL GFVKGQAQVTEVIYAPVLKQRSTEELYSLQSKLPEYLFETLSFPLSSLNQFYNKIAKSLN KKREKKDETE
>5KTB_2 Monopolin complex subunit MAM1 (chains C) QKKRFLPQSVLIKREDEIAFDDFHLDARKVLNDLSATSENPFSSSPNTKKIKSKGKTLEV VPKKKNKKII
Molecular architecture of the yeast monopolin complex. Corbett, K.D., Harrison, S.C. Cell Rep (2012) 1:583-589. DOI 10.1016/j.celrep.2012.05.012 · PubMed
Other PDB entries of the same protein (UniProt P25651 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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