Structure of Csm1 C-terminal domain, P21212 form. Determined by X-ray diffraction at 2.35 Å resolution. Released 1 Sept 2010.
Explore 3N4S in 3D Show helices and sheets RCSB PDB PDBe
3N4S contains 20 α-helices and 20 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 | 71-82 | 12 | |
| β-strand | 84-91 | 8 | 1 |
| β-strand | 96-102 | 7 | 1 |
| β-strand | 116-122 | 7 | 1 |
| β-strand | 131-137 | 7 | 1 |
| α-helix | 143-150 | 8 | |
| α-helix | 155-158 | 4 | |
| β-strand | 161-164 | 4 | 1 |
| α-helix | 165-167 | 3 | |
| α-helix | 168-179 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 72-82 | 11 | |
| β-strand | 84-88 | 5 | 2 |
| β-strand | 97-103 | 7 | 2 |
| β-strand | 115-123 | 9 | 2 |
| β-strand | 131-137 | 7 | 2 |
| α-helix | 143-152 | 10 | |
| α-helix | 155-158 | 4 | |
| β-strand | 161-164 | 4 | 2 |
| α-helix | 165-167 | 3 | |
| α-helix | 168-179 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 71-82 | 12 | |
| β-strand | 84-91 | 8 | 3 |
| β-strand | 96-103 | 8 | 3 |
| β-strand | 115-122 | 8 | 3 |
| β-strand | 131-136 | 6 | 3 |
| α-helix | 143-152 | 10 | |
| α-helix | 155-158 | 4 | |
| β-strand | 161-164 | 4 | 3 |
| α-helix | 165-167 | 3 | |
| α-helix | 168-179 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monopolin complex subunit CSM1 | A, B, C, D | protein | 116 | Saccharomyces cerevisiae | P25651 (AlphaFold model) |
>3N4S_1 Monopolin complex subunit CSM1 (chains A, B, C, D) SNAENSEVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGGSSDDYSIMDYKLGFVKG QAQVTEVIYAPVLKQRSTEELYSLQSKLPEYLFETLSFPLSSLNQFYNKIAKSLNK
The Monopolin Complex Crosslinks Kinetochore Components to Regulate Chromosome-Microtubule Attachments. Corbett, K.D., Yip, C.K., Ee, L.S. et al. Cell (2010) 142:556-567. DOI 10.1016/j.cell.2010.07.017 · 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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