crystal structure of Sfi1p/Cdc31p complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 27 Jun 2006.
Explore 2GV5 in 3D Show helices and sheets RCSB PDB PDBe
2GV5 contains 38 α-helices and 16 β-strands across 6 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 | 19-32 | 14 | |
| β-strand | 39-41 | 3 | 1 |
| α-helix | 42-52 | 11 | |
| α-helix | 58-67 | 10 | |
| β-strand | 75-77 | 3 | 1 |
| α-helix | 78-90 | 13 | |
| α-helix | 94-105 | 12 | |
| β-strand | 112-113 | 2 | 2 |
| α-helix | 115-124 | 10 | |
| α-helix | 131-139 | 9 | |
| β-strand | 149-150 | 2 | 2 |
| α-helix | 151-157 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-31 | 13 | |
| β-strand | 39-40 | 2 | 3 |
| α-helix | 42-51 | 10 | |
| α-helix | 58-68 | 11 | |
| β-strand | 76-77 | 2 | 3 |
| α-helix | 78-90 | 13 | |
| α-helix | 94-105 | 12 | |
| β-strand | 112-113 | 2 | 4 |
| α-helix | 115-125 | 11 | |
| α-helix | 131-141 | 11 | |
| β-strand | 149-150 | 2 | 4 |
| α-helix | 151-158 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 643-672 | 30 | |
| α-helix | 673-677 | 5 | |
| α-helix | 678-706 | 29 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division control protein 31 | A, B, D, E | protein | 161 | Saccharomyces cerevisiae | P06704 (AlphaFold model) |
| Sfi1p | C, F | protein | 73 | Saccharomyces cerevisiae | Q12369 (AlphaFold model) |
>2GV5_1 Cell division control protein 31 (chains A, B, D, E) MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKRE ILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRR VAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS
>2GV5_2 Sfi1p (chains C, F) GPLGSKLNDILHVYEKSKERELQSQLFNAWRNRFCFYTEECNIQAISKRNYQLEKMVLKK FRERLLEIVKSEE
Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication. Li, S., Sandercock, A.M., Conduit, P. et al. J Cell Biol (2006) 173:867-877. DOI 10.1083/jcb.200603153 · PubMed
Other PDB entries of the same protein (UniProt P06704 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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