Crystal structure of Mst1 kinase. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Apr 2008.
Explore 3COM in 3D Show helices and sheets RCSB PDB PDBe
3COM contains 40 α-helices and 30 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 |
|---|---|---|---|
| β-strand | 30-35 | 6 | 1 |
| β-strand | 43-49 | 7 | 1 |
| β-strand | 55-62 | 8 | 1 |
| α-helix | 68-78 | 11 | |
| β-strand | 85 | 1 | 2 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-94 | 7 | 1 |
| β-strand | 97-103 | 7 | 1 |
| β-strand | 108-109 | 2 | 2 |
| α-helix | 110-117 | 8 | |
| α-helix | 120-122 | 3 | |
| α-helix | 123-142 | 20 | |
| β-strand | 145-146 | 2 | 3 |
| α-helix | 152-154 | 3 | |
| β-strand | 155-157 | 3 | 2 |
| β-strand | 163-165 | 3 | 2 |
| β-strand | 172-173 | 2 | 3 |
| β-strand | 175 | 1 | 4 |
| β-strand | 178 | 1 | 4 |
| β-strand | 181 | 1 | 5 |
| α-helix | 188-190 | 3 | |
| α-helix | 193-196 | 4 | |
| β-strand | 201 | 1 | 5 |
| α-helix | 205-219 | 15 | |
| α-helix | 229-238 | 10 | |
| α-helix | 240-242 | 3 | |
| α-helix | 247-249 | 3 | |
| α-helix | 252-261 | 10 | |
| α-helix | 270-271 | 2 | |
| α-helix | 272-275 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 284-286 | 3 | |
| α-helix | 287-290 | 4 | |
| α-helix | 291-297 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-22 | 4 | |
| α-helix | 26-29 | 4 | |
| β-strand | 30-35 | 6 | 6 |
| β-strand | 44-49 | 6 | 6 |
| β-strand | 55-62 | 8 | 6 |
| α-helix | 67-77 | 11 | |
| β-strand | 85 | 1 | 7 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-94 | 7 | 6 |
| β-strand | 97-103 | 7 | 6 |
| β-strand | 108-109 | 2 | 7 |
| α-helix | 110-117 | 8 | |
| α-helix | 120-122 | 3 | |
| α-helix | 123-142 | 20 | |
| β-strand | 145-146 | 2 | 8 |
| α-helix | 152-154 | 3 | |
| β-strand | 155-157 | 3 | 7 |
| β-strand | 163-165 | 3 | 7 |
| β-strand | 172-173 | 2 | 8 |
| β-strand | 175 | 1 | 9 |
| β-strand | 178 | 1 | 9 |
| β-strand | 181 | 1 | 10 |
| α-helix | 188-190 | 3 | |
| α-helix | 193-196 | 4 | |
| β-strand | 201 | 1 | 10 |
| α-helix | 205-219 | 15 | |
| α-helix | 229-235 | 7 | |
| α-helix | 240-242 | 3 | |
| α-helix | 247-249 | 3 | |
| α-helix | 252-261 | 10 | |
| α-helix | 270-271 | 2 | |
| α-helix | 272-275 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 284-286 | 3 | |
| α-helix | 287-290 | 4 | |
| α-helix | 291-299 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase 4 | A, B | protein | 314 | Homo sapiens | Q13043 (AlphaFold model) |
>3COM_1 Serine/threonine-protein kinase 4 (chains A, B) SLETVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIK QVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNK TLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMA KRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTN PPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINEAMD VKLKRQESQQREEG
Crystal structure of Mst1 kinase. Atwell, S., Burley, S.K., Dickey, M. et al. To be published.
Other PDB entries of the same protein (UniProt Q13043 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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