Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering. Determined by solution NMR. Released 12 Jan 2011.
Explore 2L5H in 3D Show helices and sheets RCSB PDB PDBe
2L5H contains 60 α-helices and 34 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 | 8 | 1 | 1 |
| β-strand | 12-18 | 7 | 1 |
| α-helix | 33-64 | 32 | |
| α-helix | 67-80 | 14 | |
| α-helix | 83-91 | 9 | |
| α-helix | 92-96 | 5 | |
| α-helix | 100-116 | 17 | |
| α-helix | 121-142 | 22 | |
| β-strand | 156-160 | 5 | 1 |
| α-helix | 165-169 | 5 | |
| β-strand | 176-181 | 6 | 1 |
| α-helix | 189-197 | 9 | |
| β-strand | 201-202 | 2 | 1 |
| β-strand | 216-220 | 5 | 1 |
| β-strand | 227-229 | 3 | 1 |
| α-helix | 233-253 | 21 | |
| β-strand | 262 | 1 | 2 |
| β-strand | 268 | 1 | 2 |
| β-strand | 270-275 | 6 | 3 |
| α-helix | 279-287 | 9 | |
| β-strand | 292-296 | 5 | 3 |
| α-helix | 297-301 | 5 | |
| α-helix | 310-323 | 14 | |
| β-strand | 329-332 | 4 | 3 |
| α-helix | 333-334 | 2 | |
| α-helix | 343-345 | 3 | |
| α-helix | 347-349 | 3 | |
| α-helix | 353-355 | 3 | |
| α-helix | 360-363 | 4 | |
| α-helix | 367-380 | 14 | |
| β-strand | 386-390 | 5 | 3 |
| α-helix | 396-415 | 20 | |
| β-strand | 425-430 | 6 | 3 |
| α-helix | 433-437 | 5 | |
| α-helix | 439-443 | 5 | |
| β-strand | 448-451 | 4 | 3 |
| α-helix | 453-461 | 9 | |
| α-helix | 468-473 | 6 | |
| α-helix | 479-494 | 16 | |
| β-strand | 498-501 | 4 | 3 |
| α-helix | 504-507 | 4 | |
| α-helix | 512-517 | 6 | |
| β-strand | 522-525 | 4 | 3 |
| α-helix | 527-529 | 3 | |
| α-helix | 530-538 | 9 | |
| α-helix | 542-554 | 13 | |
| α-helix | 558-572 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphoenolpyruvate-protein phosphotransferase | A, B | protein | 573 | Escherichia coli | P08839 (AlphaFold model) |
>2L5H_1 Phosphoenolpyruvate-protein phosphotransferase (chains A, B) MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTK AGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFI TDAGGRTSQTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR AVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFL FMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAI RIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAF DESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPS VLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNT NFEDAKVLAEQALAQPTTDELMTLVNKFIEEKT
Combined Use of Residual Dipolar Couplings and Solution X-ray Scattering To Rapidly Probe Rigid-Body Conformational Transitions in a Non-phosphorylatable Active-Site Mutant of the 128 kDa Enzyme I Dimer. Takayama, Y., Schwieters, C.D., Grishaev, A. et al. J Am Chem Soc (2011) 133:424-427. DOI 10.1021/ja109866w · 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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