Structure of Mnk1 in complex with DS12881479. Determined by X-ray diffraction at 3.0 Å resolution. Released 3 Jan 2018.
Explore 5WVD in 3D Show helices and sheets RCSB PDB PDBe
5WVD contains 23 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 |
|---|---|---|---|
| α-helix | 44-46 | 3 | |
| β-strand | 48-57 | 10 | 1 |
| β-strand | 61-68 | 8 | 1 |
| β-strand | 74-81 | 8 | 1 |
| β-strand | 85 | 1 | 2 |
| α-helix | 87-98 | 12 | |
| β-strand | 107 | 1 | 3 |
| α-helix | 108-109 | 2 | |
| β-strand | 110-115 | 6 | 1 |
| β-strand | 119-125 | 7 | 1 |
| α-helix | 126-127 | 2 | |
| β-strand | 131 | 1 | 3 |
| α-helix | 132-139 | 8 | |
| α-helix | 144-163 | 20 | |
| β-strand | 167 | 1 | 4 |
| α-helix | 173-175 | 3 | |
| β-strand | 176-178 | 3 | 3 |
| β-strand | 187-189 | 3 | 3 |
| α-helix | 222-224 | 3 | |
| β-strand | 225 | 1 | 2 |
| β-strand | 231 | 1 | 4 |
| α-helix | 236-255 | 20 | |
| α-helix | 296-299 | 4 | |
| α-helix | 304-313 | 10 | |
| α-helix | 322-323 | 2 | |
| α-helix | 324-328 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-46 | 3 | |
| β-strand | 48-56 | 9 | 5 |
| β-strand | 61-68 | 8 | 5 |
| β-strand | 74-81 | 8 | 5 |
| β-strand | 85 | 1 | 6 |
| α-helix | 87-98 | 12 | |
| β-strand | 107 | 1 | 7 |
| α-helix | 108-109 | 2 | |
| β-strand | 110-115 | 6 | 5 |
| β-strand | 119-125 | 7 | 5 |
| β-strand | 131 | 1 | 7 |
| α-helix | 132-136 | 5 | |
| α-helix | 148-163 | 16 | |
| β-strand | 167 | 1 | 8 |
| α-helix | 173-175 | 3 | |
| β-strand | 176-178 | 3 | 7 |
| β-strand | 187-189 | 3 | 7 |
| α-helix | 222-224 | 3 | |
| β-strand | 225 | 1 | 6 |
| β-strand | 231 | 1 | 8 |
| α-helix | 236-255 | 20 | |
| α-helix | 322-323 | 2 | |
| α-helix | 324-328 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MAP kinase interacting serine/threonine kinase 1 | A, B | protein | 310 | Homo sapiens | Q9BUB5 (AlphaFold model) |
>5WVD_1 MAP kinase interacting serine/threonine kinase 1 (chains A, B) GPLGSTDSLPGKFEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRV FREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVV RDVAAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTPITTPE LTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWD RGEVCRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHP WVQGQAPEKG
| ID | Name | Formula | Copies |
|---|---|---|---|
| 7UX | 1-methyl-N-(5-phenyl-1,3-thiazol-2-yl)piperidine-4-carboxamide | C16 H19 N3 O S | 2 |
Water and common crystallization additives (SO4) are not listed.
A novel inhibitor stabilizes the inactive conformation of MAPK-interacting kinase 1. Matsui, Y., Yasumatsu, I., Yoshida, K.I. et al. Acta Crystallogr F Struct Biol Commun (2018) 74:156-160. DOI 10.1107/S2053230X18002108 · PubMed
Other PDB entries of the same protein (UniProt Q9BUB5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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