Crystal structure of the hybrid C-terminal domain of enzyme I of the bacterial phosphotransferase system formed by hybridizing the scaffold of the escherichia coli enzyme with the active site loops from the thermoanaerobacter tengcongensis enzyme. Determined by X-ray diffraction at 1.9 Å resolution. Released 17 Jun 2020.
Explore 6V9K in 3D Show helices and sheets RCSB PDB PDBe
6V9K contains 47 α-helices and 22 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 | 262 | 1 | 1 |
| β-strand | 268 | 1 | 1 |
| β-strand | 270-275 | 6 | 2 |
| α-helix | 280-286 | 7 | |
| β-strand | 292-295 | 4 | 2 |
| α-helix | 298-300 | 3 | |
| α-helix | 307-309 | 3 | |
| α-helix | 310-323 | 14 | |
| β-strand | 328-332 | 5 | 2 |
| α-helix | 333-334 | 2 | |
| α-helix | 343-345 | 3 | |
| α-helix | 347-349 | 3 | |
| α-helix | 353-355 | 3 | |
| α-helix | 360-365 | 6 | |
| α-helix | 367-380 | 14 | |
| α-helix | 381-383 | 3 | |
| β-strand | 385-390 | 6 | 2 |
| α-helix | 396-416 | 21 | |
| β-strand | 425-430 | 6 | 2 |
| α-helix | 433-437 | 5 | |
| α-helix | 439-443 | 5 | |
| β-strand | 448-451 | 4 | 2 |
| α-helix | 453-460 | 8 | |
| α-helix | 471-473 | 3 | |
| α-helix | 479-494 | 16 | |
| β-strand | 498-501 | 4 | 2 |
| α-helix | 504-507 | 4 | |
| α-helix | 512-518 | 7 | |
| β-strand | 522-525 | 4 | 2 |
| α-helix | 527-529 | 3 | |
| α-helix | 530-538 | 9 | |
| α-helix | 542-553 | 12 | |
| α-helix | 558-569 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 262 | 1 | 3 |
| β-strand | 268 | 1 | 3 |
| β-strand | 270-275 | 6 | 4 |
| α-helix | 278-280 | 3 | |
| α-helix | 281-286 | 6 | |
| β-strand | 292-295 | 4 | 4 |
| α-helix | 298-300 | 3 | |
| α-helix | 307-309 | 3 | |
| α-helix | 310-323 | 14 | |
| β-strand | 328-332 | 5 | 4 |
| α-helix | 333 | 1 | |
| β-strand | 337 | 1 | 5 |
| α-helix | 343-345 | 3 | |
| α-helix | 347-349 | 3 | |
| α-helix | 353-355 | 3 | |
| β-strand | 358 | 1 | 5 |
| α-helix | 360-365 | 6 | |
| α-helix | 367-380 | 14 | |
| α-helix | 381-383 | 3 | |
| β-strand | 385-390 | 6 | 4 |
| α-helix | 396-416 | 21 | |
| β-strand | 425-430 | 6 | 4 |
| α-helix | 433-437 | 5 | |
| α-helix | 439-442 | 4 | |
| β-strand | 448-451 | 4 | 4 |
| α-helix | 453-460 | 8 | |
| α-helix | 471-473 | 3 | |
| α-helix | 479-494 | 16 | |
| β-strand | 498-501 | 4 | 4 |
| α-helix | 504-507 | 4 | |
| α-helix | 512-518 | 7 | |
| β-strand | 522-525 | 4 | 4 |
| α-helix | 527-529 | 3 | |
| α-helix | 530-538 | 9 | |
| α-helix | 542-553 | 12 | |
| α-helix | 558-569 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphoenolpyruvate-protein phosphotransferase | A, B | protein | 316 | Escherichia coli | P08839 (AlphaFold model) |
>6V9K_1 Phosphoenolpyruvate-protein phosphotransferase (chains A, B) MAITLDGHQVEVCANIGTPKDVEGAERNGAEGVGLYRTEFLYMDRNSLPSEEEQFAAYKA VAEACGSQAVIVRTLDIGGDKELPYLDMPKEMNPFLGYRAIRIAMDRKEILRDQLRAILR ASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIA RHLAKEVDFFSIGTNDLTQYTLAVDRMNEHVKEYYQPFHPSVLNLIKQVIDASHAEGKWT GMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTD ELMTLVNKFIEEKTIC
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I. Dotas, R.R., Nguyen, T.T., Stewart Jr., C.E. et al. J Mol Biol (2020) 432:4481-4498. DOI 10.1016/j.jmb.2020.05.024 · PubMed
Other PDB entries of the same protein (UniProt P08839 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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