Crystal structure of LacY in complex with an affinity inactivator. Determined by X-ray diffraction at 3.38 Å resolution. Released 15 Jun 2011.
Explore 2Y5Y in 3D Show helices and sheets RCSB PDB PDBe
2Y5Y contains 59 α-helices and 0 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 | 7-26 | 20 | |
| α-helix | 30-32 | 3 | |
| α-helix | 33-37 | 5 | |
| α-helix | 42-69 | 28 | |
| α-helix | 71-73 | 3 | |
| α-helix | 75-85 | 11 | |
| α-helix | 88-90 | 3 | |
| α-helix | 91-95 | 5 | |
| α-helix | 96-100 | 5 | |
| α-helix | 104-119 | 16 | |
| α-helix | 121-135 | 15 | |
| α-helix | 140-175 | 36 | |
| α-helix | 176-180 | 5 | |
| α-helix | 183-186 | 4 | |
| α-helix | 210-218 | 9 | |
| α-helix | 220-228 | 9 | |
| α-helix | 229-234 | 6 | |
| α-helix | 235-241 | 7 | |
| α-helix | 243-249 | 7 | |
| α-helix | 254-286 | 33 | |
| α-helix | 288-306 | 19 | |
| α-helix | 312-325 | 14 | |
| α-helix | 327-340 | 14 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-349 | 4 | |
| α-helix | 350-357 | 8 | |
| α-helix | 358-375 | 18 | |
| α-helix | 377-399 | 23 | |
| α-helix | 401-402 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-26 | 20 | |
| α-helix | 30-32 | 3 | |
| α-helix | 33-37 | 5 | |
| α-helix | 42-69 | 28 | |
| α-helix | 71-73 | 3 | |
| α-helix | 75-85 | 11 | |
| α-helix | 88-90 | 3 | |
| α-helix | 91-95 | 5 | |
| α-helix | 96-100 | 5 | |
| α-helix | 104-112 | 9 | |
| α-helix | 116-119 | 4 | |
| α-helix | 121-135 | 15 | |
| α-helix | 140-175 | 36 | |
| α-helix | 176-180 | 5 | |
| α-helix | 181-186 | 6 | |
| α-helix | 210-218 | 9 | |
| α-helix | 220-228 | 9 | |
| α-helix | 229-234 | 6 | |
| α-helix | 235-241 | 7 | |
| α-helix | 243-249 | 7 | |
| α-helix | 254-286 | 33 | |
| α-helix | 288-306 | 19 | |
| α-helix | 312-325 | 14 | |
| α-helix | 327-340 | 14 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-349 | 4 | |
| α-helix | 350-357 | 8 | |
| α-helix | 358-375 | 18 | |
| α-helix | 377-395 | 19 | |
| α-helix | 396-398 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lactose permease | A, B | protein | 423 | ESCHERICHIA COLI | P02920 (AlphaFold model) |
>2Y5Y_1 LACTOSE PERMEASE (chains A, B) MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQ PLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFSFNA GCPAVEAFIEKVSRRSNFEFGRARMFGAVGWALVASIVGIMFTINNQFVFWLGSGMALIL AVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSSTYDVFD QQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMS VRIIGSSFATSALEVVILKTLHMFEVPFLLVGSFKYITSQFEVRFSATIYLVAFAFFKQL AMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVAHHH HHH
Crystal Structure of Lactose Permease in Complex with an Affinity Inactivator Yields Unique Insight Into Sugar Recognition. Chaptal, V., Kwon, S., Sawaya, M.R. et al. Proc Natl Acad Sci U S A (2011) 108:9361. DOI 10.1073/PNAS.1105687108 · PubMed
Other PDB entries of the same protein (UniProt P02920 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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