Crystal structure of MST2 in complex with XMU-MP-1. Determined by X-ray diffraction at 1.9 Å resolution. Released 20 Jul 2022.
Explore 8A66 in 3D Show helices and sheets RCSB PDB PDBe
8A66 contains 41 α-helices and 26 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 | 129-134 | 6 | 1 |
| α-helix | 135 | 1 | |
| β-strand | 143-148 | 6 | 1 |
| β-strand | 154-160 | 7 | 1 |
| α-helix | 166-177 | 12 | |
| β-strand | 184 | 1 | 2 |
| α-helix | 185-186 | 2 | |
| β-strand | 187-193 | 7 | 1 |
| β-strand | 196-202 | 7 | 1 |
| β-strand | 207-208 | 2 | 2 |
| α-helix | 209-216 | 8 | |
| α-helix | 219-221 | 3 | |
| α-helix | 222-241 | 20 | |
| β-strand | 244-245 | 2 | 3 |
| α-helix | 251-253 | 3 | |
| β-strand | 254-256 | 3 | 2 |
| β-strand | 262-264 | 3 | 2 |
| β-strand | 271-272 | 2 | 3 |
| β-strand | 280 | 1 | 4 |
| α-helix | 287-289 | 3 | |
| α-helix | 292-295 | 4 | |
| β-strand | 300 | 1 | 4 |
| α-helix | 304-318 | 15 | |
| α-helix | 328-334 | 7 | |
| α-helix | 339-341 | 3 | |
| α-helix | 346-348 | 3 | |
| α-helix | 351-360 | 10 | |
| α-helix | 365-367 | 3 | |
| α-helix | 369-370 | 2 | |
| α-helix | 371-374 | 4 | |
| α-helix | 378-381 | 4 | |
| α-helix | 383-385 | 3 | |
| α-helix | 386-389 | 4 | |
| α-helix | 390-404 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 125-128 | 4 | |
| β-strand | 129-136 | 8 | 5 |
| β-strand | 143-148 | 6 | 5 |
| β-strand | 153-160 | 8 | 5 |
| α-helix | 166-178 | 13 | |
| β-strand | 184 | 1 | 6 |
| β-strand | 187-193 | 7 | 5 |
| β-strand | 196-202 | 7 | 5 |
| β-strand | 207-208 | 2 | 6 |
| α-helix | 209-216 | 8 | |
| α-helix | 219-221 | 3 | |
| α-helix | 222-241 | 20 | |
| β-strand | 244-245 | 2 | 7 |
| α-helix | 251-253 | 3 | |
| β-strand | 254-256 | 3 | 6 |
| β-strand | 262-264 | 3 | 6 |
| β-strand | 271-272 | 2 | 7 |
| β-strand | 281 | 1 | 8 |
| α-helix | 288-290 | 3 | |
| α-helix | 293-296 | 4 | |
| β-strand | 301 | 1 | 8 |
| α-helix | 305-319 | 15 | |
| α-helix | 329-335 | 7 | |
| α-helix | 340-342 | 3 | |
| α-helix | 347-349 | 3 | |
| α-helix | 352-361 | 10 | |
| α-helix | 366-368 | 3 | |
| α-helix | 370-371 | 2 | |
| α-helix | 373-376 | 4 | |
| α-helix | 380-383 | 4 | |
| α-helix | 385-387 | 3 | |
| α-helix | 388-391 | 4 | |
| α-helix | 392-407 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase 3 36kDa subunit | A | protein | 298 | Homo sapiens | Q13188 (AlphaFold model) |
| Serine/threonine-protein kinase 3 36kDa subunit | B | protein | 298 | Homo sapiens | Q13188 (AlphaFold model) |
>8A66_1 Serine/threonine-protein kinase 3 36kDa subunit (chains A) GEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIM QQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGL EYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQ EIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDF VKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEE
>8A66_2 Serine/threonine-protein kinase 3 36kDa subunit (chains B) GEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIM QQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGL EYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQ EIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDF VKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| 5BS | 4-[(5,10-dimethyl-6-oxo-6,10-dihydro-5H-pyrimido[5,4-b]thieno[3,2-e][1,4]diazep… | C17 H16 N6 O3 S2 | 2 |
Water and common crystallization additives (NA) are not listed.
Crystal structure of the Kelch domain of human Keap1in complex with ligand S217879. Weber, C., Vuillard, L., Delerive, P. et al. To be published.
Other PDB entries of the same protein (UniProt Q13188 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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