Crystal structure of the C-terminal domain of enzyme I of the bacterial phosphotransferase system from the escherichia coli enzyme. Determined by X-ray diffraction at 3.5 Å resolution. Released 17 Jun 2020.
Explore 6VU0 in 3D Show helices and sheets RCSB PDB PDBe
6VU0 contains 42 α-helices and 20 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 | 278-286 | 9 | |
| β-strand | 292-296 | 5 | 2 |
| α-helix | 298-301 | 4 | |
| α-helix | 307-309 | 3 | |
| α-helix | 310-324 | 15 | |
| β-strand | 328-332 | 5 | 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 | 425-428 | 4 | 2 |
| α-helix | 433-437 | 5 | |
| α-helix | 439-443 | 5 | |
| β-strand | 448-450 | 3 | 2 |
| α-helix | 453-461 | 9 | |
| α-helix | 471-473 | 3 | |
| α-helix | 479-494 | 16 | |
| β-strand | 498-501 | 4 | 2 |
| α-helix | 504-507 | 4 | |
| α-helix | 509-517 | 9 | |
| β-strand | 522-526 | 5 | 2 |
| α-helix | 527-529 | 3 | |
| α-helix | 530-538 | 9 | |
| α-helix | 542-552 | 11 | |
| 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 | 281-286 | 6 | |
| β-strand | 292-296 | 5 | 4 |
| α-helix | 298-301 | 4 | |
| α-helix | 310-324 | 15 | |
| β-strand | 328-332 | 5 | 4 |
| α-helix | 343-345 | 3 | |
| α-helix | 347-349 | 3 | |
| α-helix | 353-355 | 3 | |
| α-helix | 359-365 | 7 | |
| α-helix | 368-380 | 13 | |
| α-helix | 381-383 | 3 | |
| β-strand | 385-390 | 6 | 4 |
| α-helix | 396-415 | 20 | |
| β-strand | 425-428 | 4 | 4 |
| α-helix | 433-437 | 5 | |
| α-helix | 439-443 | 5 | |
| β-strand | 448-451 | 4 | 4 |
| α-helix | 453-461 | 9 | |
| α-helix | 471-473 | 3 | |
| α-helix | 479-494 | 16 | |
| β-strand | 498-501 | 4 | 4 |
| α-helix | 504-507 | 4 | |
| α-helix | 509-517 | 9 | |
| β-strand | 522-525 | 4 | 4 |
| α-helix | 530-538 | 9 | |
| α-helix | 542-552 | 11 | |
| α-helix | 558-568 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PEP-protein phosphotransferase system enzyme I | A, B | protein | 316 | Escherichia coli | P08839 (AlphaFold model) |
>6VU0_1 PEP-protein phosphotransferase system enzyme I (chains A, B) MAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKA VAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAIRIAMDRREILRDQLRAILR ASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIA RHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWT GMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTD ELMTLVNKFIEEKTIC
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:
MolViewer shows 6VU0 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.