Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase. Determined by X-ray diffraction at 2.6 Å resolution. Released 31 Oct 1993.
Explore 1GLB in 3D Show helices and sheets RCSB PDB PDBe
1GLB contains 24 α-helices and 47 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 | 7-9 | 3 | |
| β-strand | 20-23 | 4 | 1 |
| β-strand | 28-32 | 5 | 2 |
| α-helix | 33-35 | 3 | |
| α-helix | 39-42 | 4 | |
| β-strand | 48-54 | 7 | 2 |
| β-strand | 58-60 | 3 | 3 |
| β-strand | 65-70 | 6 | 2 |
| β-strand | 76-81 | 6 | 2 |
| β-strand | 85-90 | 6 | 2 |
| β-strand | 93 | 1 | 4 |
| α-helix | 96-98 | 3 | |
| β-strand | 101 | 1 | 3 |
| β-strand | 103-105 | 3 | 3 |
| β-strand | 112-113 | 2 | 2 |
| β-strand | 118-122 | 5 | 3 |
| α-helix | 124-130 | 7 | |
| β-strand | 133 | 1 | 4 |
| β-strand | 138-140 | 3 | 2 |
| α-helix | 143-145 | 3 | |
| β-strand | 148-151 | 4 | 1 |
| β-strand | 155-156 | 2 | 2 |
| β-strand | 162-167 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-11 | 7 | 5 |
| β-strand | 15-21 | 7 | 5 |
| β-strand | 27-34 | 8 | 5 |
| β-strand | 38 | 1 | 6 |
| β-strand | 46-47 | 2 | 6 |
| α-helix | 49-66 | 18 | |
| β-strand | 74-81 | 8 | 5 |
| β-strand | 86-90 | 5 | 6 |
| β-strand | 96 | 1 | 6 |
| β-strand | 100-101 | 2 | 6 |
| α-helix | 109-117 | 9 | |
| α-helix | 121-128 | 8 | |
| α-helix | 138-147 | 10 | |
| α-helix | 151-156 | 6 | |
| β-strand | 160-164 | 5 | 6 |
| α-helix | 165-173 | 9 | |
| β-strand | 180-181 | 2 | 7 |
| α-helix | 183-187 | 5 | |
| β-strand | 192-193 | 2 | 8 |
| β-strand | 198-199 | 2 | 8 |
| β-strand | 216-217 | 2 | 7 |
| β-strand | 221-226 | 6 | 5 |
| β-strand | 238-244 | 7 | 5 |
| α-helix | 245-252 | 8 | |
| β-strand | 261-265 | 5 | 9 |
| β-strand | 269-276 | 8 | 9 |
| α-helix | 280-282 | 3 | |
| β-strand | 287-292 | 6 | 9 |
| β-strand | 298-306 | 9 | 9 |
| α-helix | 311-318 | 8 | |
| α-helix | 328-333 | 6 | |
| β-strand | 343-345 | 3 | 10 |
| β-strand | 348 | 1 | 11 |
| β-strand | 350 | 1 | 11 |
| β-strand | 351 | 1 | 12 |
| β-strand | 357 | 1 | 12 |
| β-strand | 363-365 | 3 | 10 |
| α-helix | 373-398 | 26 | |
| β-strand | 405-407 | 3 | 13 |
| β-strand | 408-410 | 3 | 9 |
| α-helix | 412-414 | 3 | |
| α-helix | 416-426 | 11 | |
| β-strand | 429-432 | 4 | 13 |
| α-helix | 438-450 | 13 | |
| α-helix | 457-459 | 3 | |
| β-strand | 468-470 | 3 | 13 |
| α-helix | 474-477 | 4 | |
| α-helix | 479-493 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucose-specific protein iiiglc | F | protein | 168 | Escherichia coli | P69783 (AlphaFold model) |
| Glycerol kinase | G | protein | 501 | Escherichia coli | P0A6F3 (AlphaFold model) |
>1GLB_1 GLUCOSE-SPECIFIC PROTEIN IIIGlc (chains F) GLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMV APVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVI EFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK
>1GLB_2 GLYCEROL KINASE (chains G) TEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTL VEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGL EDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHV TDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPIS GIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNY ALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYA RGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQ FQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERN YRYAGWKKAVKRAMAWEEHDE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Water and common crystallization additives (GOL) are not listed.
Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Hurley, J.H., Faber, H.R., Worthylake, D. et al. Science (1993) 259:673-677. PubMed
Other PDB entries of the same protein (UniProt P69783 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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