Crystal structure of lactose permease with TDG. Determined by X-ray diffraction at 3.6 Å resolution. Released 12 Aug 2003.
Explore 1PV7 in 3D Show helices and sheets RCSB PDB PDBe
1PV7 contains 55 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 | 2-5 | 4 | |
| α-helix | 7-38 | 32 | |
| α-helix | 42-58 | 17 | |
| α-helix | 60-70 | 11 | |
| α-helix | 75-85 | 11 | |
| α-helix | 87-89 | 3 | |
| α-helix | 90-95 | 6 | |
| α-helix | 96-100 | 5 | |
| α-helix | 104-109 | 6 | |
| α-helix | 114-118 | 5 | |
| α-helix | 121-136 | 16 | |
| α-helix | 140-164 | 25 | |
| α-helix | 166-185 | 20 | |
| α-helix | 199-202 | 4 | |
| α-helix | 210-216 | 7 | |
| α-helix | 221-226 | 6 | |
| α-helix | 227-233 | 7 | |
| α-helix | 234-247 | 14 | |
| α-helix | 254-276 | 23 | |
| α-helix | 279-286 | 8 | |
| α-helix | 288-307 | 20 | |
| α-helix | 312-340 | 29 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-348 | 3 | |
| α-helix | 349-355 | 7 | |
| α-helix | 358-376 | 19 | |
| α-helix | 378-399 | 22 | |
| α-helix | 408-416 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-5 | 4 | |
| α-helix | 7-38 | 32 | |
| α-helix | 42-58 | 17 | |
| α-helix | 60-69 | 10 | |
| α-helix | 75-85 | 11 | |
| α-helix | 87-90 | 4 | |
| α-helix | 91-95 | 5 | |
| α-helix | 96-100 | 5 | |
| α-helix | 104-109 | 6 | |
| α-helix | 114-118 | 5 | |
| α-helix | 121-136 | 16 | |
| α-helix | 140-164 | 25 | |
| α-helix | 166-185 | 20 | |
| α-helix | 199-202 | 4 | |
| α-helix | 210-216 | 7 | |
| α-helix | 221-228 | 8 | |
| α-helix | 229-234 | 6 | |
| α-helix | 235-247 | 13 | |
| α-helix | 254-286 | 33 | |
| α-helix | 288-307 | 20 | |
| α-helix | 312-340 | 29 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-348 | 3 | |
| α-helix | 349-355 | 7 | |
| α-helix | 358-376 | 19 | |
| α-helix | 378-399 | 22 | |
| α-helix | 408-416 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lactose permease | A, B | protein | 417 | Escherichia coli | P02920 (AlphaFold model) |
>1PV7_1 Lactose permease (chains A, B) MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQ PLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNA GAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALGASIVGIMFTINNQFVFWLGSGCALIL AVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD QQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMS VRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQL AMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA
Structure and mechanism of the lactose permease of Escherichia coli. Abramson, J., Smirnova, I., Kasho, V. et al. Science (2003) 301:610-615. DOI 10.1126/science.1088196 · 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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