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 1GLA in 3D Show helices and sheets RCSB PDB PDBe
1GLA contains 23 α-helices and 48 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 | 20-23 | 4 | 1 |
| β-strand | 28-31 | 4 | 2 |
| α-helix | 33-35 | 3 | |
| α-helix | 39-42 | 4 | |
| β-strand | 48-50 | 3 | 3 |
| β-strand | 51-54 | 4 | 2 |
| β-strand | 58-60 | 3 | 4 |
| β-strand | 65-70 | 6 | 3 |
| β-strand | 76-81 | 6 | 3 |
| β-strand | 86-90 | 5 | 3 |
| β-strand | 93 | 1 | 5 |
| α-helix | 95-98 | 4 | |
| β-strand | 103-105 | 3 | 4 |
| β-strand | 112-113 | 2 | 3 |
| β-strand | 118-122 | 5 | 4 |
| α-helix | 124-130 | 7 | |
| β-strand | 133 | 1 | 5 |
| β-strand | 138-140 | 3 | 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 | 6 |
| β-strand | 15-21 | 7 | 6 |
| β-strand | 27-34 | 8 | 6 |
| β-strand | 38 | 1 | 7 |
| β-strand | 46-47 | 2 | 7 |
| α-helix | 49-67 | 19 | |
| β-strand | 74-81 | 8 | 6 |
| β-strand | 86 | 1 | 7 |
| β-strand | 87-90 | 4 | 8 |
| β-strand | 96 | 1 | 8 |
| β-strand | 100-101 | 2 | 7 |
| α-helix | 109-118 | 10 | |
| α-helix | 121-128 | 8 | |
| α-helix | 137-147 | 11 | |
| α-helix | 151-154 | 4 | |
| β-strand | 160-163 | 4 | 8 |
| α-helix | 165-173 | 9 | |
| β-strand | 180-182 | 3 | 9 |
| α-helix | 183-187 | 5 | |
| β-strand | 192 | 1 | 10 |
| β-strand | 199 | 1 | 10 |
| α-helix | 203-206 | 4 | |
| β-strand | 216-218 | 3 | 9 |
| β-strand | 221-226 | 6 | 6 |
| β-strand | 238-244 | 7 | 6 |
| α-helix | 247-252 | 6 | |
| β-strand | 260-265 | 6 | 11 |
| β-strand | 269-274 | 6 | 11 |
| α-helix | 280-282 | 3 | |
| β-strand | 287-292 | 6 | 11 |
| β-strand | 298-306 | 9 | 11 |
| α-helix | 310-318 | 9 | |
| α-helix | 328-333 | 6 | |
| β-strand | 343-345 | 3 | 12 |
| β-strand | 348 | 1 | 13 |
| β-strand | 350 | 1 | 13 |
| β-strand | 352 | 1 | 11 |
| β-strand | 356 | 1 | 11 |
| β-strand | 363-365 | 3 | 12 |
| α-helix | 373-399 | 27 | |
| β-strand | 406-407 | 2 | 14 |
| β-strand | 408-410 | 3 | 11 |
| α-helix | 411-414 | 4 | |
| α-helix | 416-426 | 11 | |
| β-strand | 430-433 | 4 | 14 |
| α-helix | 439-451 | 13 | |
| α-helix | 457-460 | 4 | |
| β-strand | 466-470 | 5 | 14 |
| α-helix | 474-478 | 5 | |
| 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) |
>1GLA_1 GLUCOSE-SPECIFIC PROTEIN IIIGlc (chains F) GLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTGNKMV APVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVGDTVI EFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK
>1GLA_2 GLYCEROL KINASE (chains G) TEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTL VEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGL EDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHV TDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPIS GIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNY ALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYA RGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQ FQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERN YRYAGWKKAVKRAMAWEEHDE
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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