N-acetylglucosamine kinase from Plesiomonas shigelloides compexed with alpha-N-acetylglucosamine. Determined by X-ray diffraction at 1.94 Å resolution. Released 10 Aug 2022.
Explore 7P9Y in 3D Show helices and sheets RCSB PDB PDBe
7P9Y contains 32 α-helices and 34 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 | 2-7 | 6 | 1 |
| β-strand | 11-17 | 7 | 1 |
| β-strand | 23-30 | 8 | 1 |
| α-helix | 36-53 | 18 | |
| β-strand | 59-64 | 6 | 1 |
| β-strand | 67-68 | 2 | 2 |
| β-strand | 75-76 | 2 | 2 |
| α-helix | 88-95 | 8 | |
| β-strand | 100-104 | 5 | 1 |
| α-helix | 105-114 | 10 | |
| β-strand | 124-130 | 7 | 3 |
| β-strand | 134-140 | 7 | 3 |
| β-strand | 143-145 | 3 | 3 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 4 |
| α-helix | 160 | 1 | |
| β-strand | 161 | 1 | 5 |
| α-helix | 162-167 | 6 | |
| α-helix | 170-172 | 3 | |
| β-strand | 177 | 1 | 6 |
| β-strand | 183 | 1 | 6 |
| β-strand | 185 | 1 | 4 |
| α-helix | 186-188 | 3 | |
| α-helix | 192-203 | 12 | |
| α-helix | 209-217 | 9 | |
| α-helix | 221-245 | 25 | |
| β-strand | 249-253 | 5 | 3 |
| α-helix | 255-258 | 4 | |
| α-helix | 261-269 | 9 | |
| α-helix | 280-281 | 2 | |
| β-strand | 282-285 | 4 | 3 |
| α-helix | 292-298 | 7 | |
| α-helix | 299-301 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 7 |
| β-strand | 11-17 | 7 | 7 |
| β-strand | 23-30 | 8 | 7 |
| α-helix | 36-53 | 18 | |
| β-strand | 59-64 | 6 | 7 |
| β-strand | 67-68 | 2 | 8 |
| β-strand | 75-76 | 2 | 8 |
| α-helix | 88-94 | 7 | |
| β-strand | 100-104 | 5 | 7 |
| α-helix | 105-114 | 10 | |
| β-strand | 124-130 | 7 | 9 |
| β-strand | 134-140 | 7 | 9 |
| β-strand | 143-145 | 3 | 9 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 10 |
| α-helix | 160 | 1 | |
| β-strand | 161 | 1 | 5 |
| α-helix | 162-167 | 6 | |
| α-helix | 170-172 | 3 | |
| β-strand | 177 | 1 | 11 |
| β-strand | 183 | 1 | 11 |
| β-strand | 185 | 1 | 10 |
| α-helix | 186-188 | 3 | |
| α-helix | 192-203 | 12 | |
| α-helix | 209-217 | 9 | |
| α-helix | 221-245 | 25 | |
| β-strand | 249-253 | 5 | 9 |
| α-helix | 255-258 | 4 | |
| α-helix | 261-269 | 9 | |
| α-helix | 280-281 | 2 | |
| β-strand | 282-285 | 4 | 9 |
| α-helix | 292-298 | 7 | |
| α-helix | 299-301 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase | AAA, BBB | protein | 417 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Plesiomonas shigelloides 302-73 | Q12306 (AlphaFold model), R8APY9 (AlphaFold model) |
>7P9Y_1 Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase (chains AAA, BBB) MAHHHHHHGSDSEVNQEAKPEVKPEVKPETHINLKVSDGSSEIFFKIKKTTPLRRLMEAF AKRQGKEMDSLRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQISSGLEVLFQGTMYYGF DIGGTKIEFGAFDADLVRVARERVATPTESYAAFLDAIVTLVNNADAEFGVKGTVGIGIP GIADVETGKLLTSNIPAAMGHTLQRDLEERLQRPVKIENDANCFALSEAWDEDLRGEPSV LGLILGTGVGGGLIFNGKVHSGRANIAGEIGHTRLPYDALKLLGMENAPIFPCGCKNSGC IDNYLSGRGFEQLYDHYFSEKLSAPEIIAHYEQGERRAVQHVERFMELLAICLANIFTCL DPHVVVLGGGLSNFELIYQELPKRLPAHLLHVAKLPKIIKARHGDAGGVRGAAFLNL
Water and common crystallization additives (K, PEG, CL, PGE, EDO, MPD) are not listed.
Spinning sugars in antigen biosynthesis: characterization of the Coxiella burnetii and Streptomyces griseus TDP-sugar epimerases. Cross, A.R., Roy, S., Vivoli Vega, M. et al. J Biol Chem (2022). DOI 10.1016/j.jbc.2022.101903
Other PDB entries of the same protein (UniProt Q12306 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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