Crystal structure of Mnk1 catalytic domain. Determined by X-ray diffraction at 2.5 Å resolution. Released 29 Aug 2006.
Explore 2HW6 in 3D Show helices and sheets RCSB PDB PDBe
2HW6 contains 24 α-helices and 27 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 | 87-101 | 15 | |
| 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 | 1 | |
| 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 |
| β-strand | 225 | 1 | 2 |
| α-helix | 226-228 | 3 | |
| 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 | 324-329 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-43 | 3 | |
| α-helix | 44-46 | 3 | |
| β-strand | 48-50 | 3 | 5 |
| α-helix | 51 | 1 | |
| β-strand | 56-57 | 2 | 5 |
| β-strand | 61-68 | 8 | 5 |
| β-strand | 74-81 | 8 | 5 |
| β-strand | 85 | 1 | 6 |
| α-helix | 87-99 | 13 | |
| β-strand | 107 | 1 | 7 |
| β-strand | 110-115 | 6 | 5 |
| β-strand | 119-125 | 7 | 5 |
| β-strand | 130-131 | 2 | 7 |
| α-helix | 134-137 | 4 | |
| α-helix | 144-163 | 20 | |
| β-strand | 167 | 1 | 8 |
| α-helix | 173-175 | 3 | |
| β-strand | 176-178 | 3 | 7 |
| β-strand | 188-189 | 2 | 7 |
| β-strand | 225 | 1 | 6 |
| β-strand | 231 | 1 | 8 |
| α-helix | 236-255 | 20 | |
| α-helix | 304-311 | 8 | |
| α-helix | 322-323 | 2 | |
| α-helix | 324-327 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MAP kinase-interacting serine/threonine-protein kinase 1 | A, B | protein | 307 | Homo sapiens | Q9BUB5 (AlphaFold model) |
>2HW6_1 MAP kinase-interacting serine/threonine-protein kinase 1 (chains A, B) GSTDSLPGKFEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFRE VETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDV AAALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTPITTPELTT PCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGE VCRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQ GQAPEKG
Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment. Jauch, R., Cho, M.K., Netter, C. et al. EMBO J (2006) 25:4020-4032. DOI 10.1038/sj.emboj.7601285 · 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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