Crystal structure of E. coli lactose permease G46W,G262W bound to sugar. Determined by X-ray diffraction at 3.5 Å resolution. Released 29 Jan 2014.
Explore 4OAA in 3D Show helices and sheets RCSB PDB PDBe
4OAA contains 62 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 | 7-24 | 18 | |
| α-helix | 30-32 | 3 | |
| α-helix | 33-37 | 5 | |
| α-helix | 49-57 | 9 | |
| α-helix | 60-68 | 9 | |
| α-helix | 75-83 | 9 | |
| α-helix | 84-86 | 3 | |
| α-helix | 87-89 | 3 | |
| α-helix | 90-94 | 5 | |
| α-helix | 95-101 | 7 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-112 | 4 | |
| α-helix | 113-114 | 2 | |
| α-helix | 115-119 | 5 | |
| α-helix | 122-135 | 14 | |
| α-helix | 140-164 | 25 | |
| α-helix | 168-185 | 18 | |
| α-helix | 210-217 | 8 | |
| α-helix | 220-228 | 9 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-239 | 6 | |
| α-helix | 243-248 | 6 | |
| α-helix | 254-286 | 33 | |
| α-helix | 289-307 | 19 | |
| α-helix | 312-340 | 29 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-349 | 4 | |
| α-helix | 350-356 | 7 | |
| α-helix | 357-373 | 17 | |
| α-helix | 379-395 | 17 | |
| α-helix | 405-408 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-24 | 18 | |
| α-helix | 30-32 | 3 | |
| α-helix | 33-38 | 6 | |
| α-helix | 45-52 | 8 | |
| α-helix | 56-69 | 14 | |
| α-helix | 75-83 | 9 | |
| α-helix | 84-86 | 3 | |
| α-helix | 87-89 | 3 | |
| α-helix | 90-94 | 5 | |
| α-helix | 95-100 | 6 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 113-114 | 2 | |
| α-helix | 115-119 | 5 | |
| α-helix | 121-135 | 15 | |
| α-helix | 140-165 | 26 | |
| α-helix | 168-186 | 19 | |
| α-helix | 211-218 | 8 | |
| α-helix | 220-228 | 9 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-239 | 6 | |
| α-helix | 243-248 | 6 | |
| α-helix | 254-286 | 33 | |
| α-helix | 289-305 | 17 | |
| α-helix | 312-338 | 27 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-350 | 5 | |
| α-helix | 352-357 | 6 | |
| α-helix | 358-376 | 19 | |
| α-helix | 378-399 | 22 | |
| α-helix | 405-409 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lactose/galactose transporter | A, B | protein | 417 | Escherichia coli | P02920 (AlphaFold model) |
>4OAA_1 Lactose/galactose transporter (chains A, B) MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTWIIFAAISLFSLLFQ PLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNA GAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALIL AVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD QQFANFFTSFFATGEQGTRVFWYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMS VRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQL AMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA
Structure of sugar-bound LacY. Kumar, H., Kasho, V., Smirnova, I. et al. Proc Natl Acad Sci U S A (2014) 111:1784-1788. DOI 10.1073/pnas.1324141111 · 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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