Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. Determined by X-ray diffraction at 3.05 Å resolution. Released 19 Jan 1999.
Explore 1BOT in 3D Show helices and sheets RCSB PDB PDBe
1BOT contains 39 α-helices and 58 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 | 5-11 | 7 | 1 |
| β-strand | 15-22 | 8 | 1 |
| β-strand | 27-34 | 8 | 1 |
| β-strand | 38 | 1 | 2 |
| β-strand | 46-47 | 2 | 2 |
| α-helix | 49-66 | 18 | |
| α-helix | 71-73 | 3 | |
| β-strand | 74-81 | 8 | 1 |
| β-strand | 86-90 | 5 | 2 |
| β-strand | 96-101 | 6 | 2 |
| α-helix | 110-118 | 9 | |
| α-helix | 121-128 | 8 | |
| α-helix | 137-147 | 11 | |
| α-helix | 151-156 | 6 | |
| β-strand | 160-163 | 4 | 2 |
| α-helix | 165-174 | 10 | |
| β-strand | 180-182 | 3 | 3 |
| α-helix | 183-186 | 4 | |
| β-strand | 192 | 1 | 4 |
| β-strand | 199 | 1 | 4 |
| α-helix | 201-203 | 3 | |
| α-helix | 204-208 | 5 | |
| α-helix | 211-213 | 3 | |
| β-strand | 216-218 | 3 | 3 |
| β-strand | 221-227 | 7 | 1 |
| β-strand | 237-244 | 8 | 1 |
| α-helix | 245-252 | 8 | |
| β-strand | 261-265 | 5 | 5 |
| β-strand | 269-274 | 6 | 5 |
| β-strand | 287-292 | 6 | 5 |
| β-strand | 298-306 | 9 | 5 |
| α-helix | 310-318 | 9 | |
| α-helix | 329-333 | 5 | |
| β-strand | 343-345 | 3 | 6 |
| β-strand | 348 | 1 | 7 |
| β-strand | 350 | 1 | 7 |
| β-strand | 352 | 1 | 5 |
| β-strand | 363-365 | 3 | 6 |
| α-helix | 373-399 | 27 | |
| β-strand | 405-407 | 3 | 8 |
| β-strand | 408-409 | 2 | 5 |
| α-helix | 411-414 | 4 | |
| α-helix | 416-426 | 11 | |
| β-strand | 429-433 | 5 | 8 |
| α-helix | 438-449 | 12 | |
| β-strand | 466-470 | 5 | 8 |
| α-helix | 476-493 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-11 | 7 | 9 |
| β-strand | 15-22 | 8 | 9 |
| β-strand | 27-34 | 8 | 9 |
| β-strand | 38 | 1 | 10 |
| β-strand | 42 | 1 | 11 |
| β-strand | 44 | 1 | 11 |
| β-strand | 46-47 | 2 | 10 |
| α-helix | 49-66 | 18 | |
| α-helix | 71-73 | 3 | |
| β-strand | 74-81 | 8 | 9 |
| β-strand | 86-90 | 5 | 10 |
| β-strand | 96-101 | 6 | 10 |
| α-helix | 102 | 1 | |
| α-helix | 109-117 | 9 | |
| α-helix | 121-127 | 7 | |
| α-helix | 137-147 | 11 | |
| α-helix | 152-157 | 6 | |
| β-strand | 160-164 | 5 | 10 |
| α-helix | 165-173 | 9 | |
| β-strand | 180-182 | 3 | 12 |
| α-helix | 183-186 | 4 | |
| β-strand | 192-193 | 2 | 13 |
| β-strand | 198-199 | 2 | 13 |
| α-helix | 201-207 | 7 | |
| β-strand | 216-218 | 3 | 12 |
| β-strand | 225-228 | 4 | 9 |
| β-strand | 236-244 | 9 | 9 |
| α-helix | 245-252 | 8 | |
| β-strand | 261-265 | 5 | 14 |
| β-strand | 269-276 | 8 | 14 |
| β-strand | 287-293 | 7 | 14 |
| β-strand | 297-306 | 10 | 14 |
| α-helix | 310-314 | 5 | |
| α-helix | 315-319 | 5 | |
| α-helix | 329-334 | 6 | |
| β-strand | 343-345 | 3 | 15 |
| β-strand | 348 | 1 | 16 |
| β-strand | 350 | 1 | 16 |
| β-strand | 352 | 1 | 14 |
| β-strand | 363-365 | 3 | 15 |
| α-helix | 373-399 | 27 | |
| β-strand | 405-407 | 3 | 17 |
| β-strand | 408-409 | 2 | 14 |
| α-helix | 411-414 | 4 | |
| α-helix | 416-426 | 11 | |
| β-strand | 429-433 | 5 | 17 |
| α-helix | 438-450 | 13 | |
| α-helix | 457-460 | 4 | |
| β-strand | 466-470 | 5 | 17 |
| α-helix | 476-493 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (glycerol kinase) | O, Z | protein | 501 | Escherichia coli | P0A6F3 (AlphaFold model) |
>1BOT_1 PROTEIN (GLYCEROL KINASE) (chains O, Z) TEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTL VEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGL EDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHV TDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPIS GIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNY ALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYA RGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQ FQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERN YRYAGWKKAVKRAMAWEEHDE
Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate. Ormo, M., Bystrom, C.E., Remington, S.J. Biochemistry (1998) 37:16565-16572. DOI 10.1021/bi981616s · PubMed
Other PDB entries of the same protein (UniProt P0A6F3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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