Wild-type Structure of Lactose Permease. Determined by X-ray diffraction at 3.6 Å resolution. Released 11 Sept 2007.
Explore 2V8N in 3D Show helices and sheets RCSB PDB PDBe
2V8N contains 66 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 | 7-38 | 32 | |
| α-helix | 42-45 | 4 | |
| α-helix | 48-57 | 10 | |
| α-helix | 60-63 | 4 | |
| α-helix | 64-68 | 5 | |
| α-helix | 77-84 | 8 | |
| α-helix | 91-95 | 5 | |
| α-helix | 96-99 | 4 | |
| α-helix | 104-109 | 6 | |
| α-helix | 112-114 | 3 | |
| α-helix | 122-136 | 15 | |
| α-helix | 149-158 | 10 | |
| α-helix | 161-164 | 4 | |
| α-helix | 166-175 | 10 | |
| α-helix | 178-183 | 6 | |
| α-helix | 210-216 | 7 | |
| α-helix | 220-227 | 8 | |
| α-helix | 228-233 | 6 | |
| α-helix | 234-240 | 7 | |
| α-helix | 244-249 | 6 | |
| α-helix | 254-263 | 10 | |
| α-helix | 265-286 | 22 | |
| α-helix | 288-308 | 21 | |
| α-helix | 317-320 | 4 | |
| α-helix | 326-337 | 12 | |
| α-helix | 338-340 | 3 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-348 | 3 | |
| α-helix | 349-353 | 5 | |
| α-helix | 358-376 | 19 | |
| α-helix | 378-388 | 11 | |
| α-helix | 390-393 | 4 | |
| α-helix | 396-399 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-38 | 32 | |
| α-helix | 42-45 | 4 | |
| α-helix | 48-57 | 10 | |
| α-helix | 60-63 | 4 | |
| α-helix | 64-68 | 5 | |
| α-helix | 77-84 | 8 | |
| α-helix | 91-95 | 5 | |
| α-helix | 96-99 | 4 | |
| α-helix | 104-109 | 6 | |
| α-helix | 112-114 | 3 | |
| α-helix | 122-136 | 15 | |
| α-helix | 149-158 | 10 | |
| α-helix | 161-164 | 4 | |
| α-helix | 166-175 | 10 | |
| α-helix | 178-183 | 6 | |
| α-helix | 210-216 | 7 | |
| α-helix | 220-228 | 9 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-240 | 7 | |
| α-helix | 244-249 | 6 | |
| α-helix | 254-263 | 10 | |
| α-helix | 265-286 | 22 | |
| α-helix | 288-308 | 21 | |
| α-helix | 317-320 | 4 | |
| α-helix | 326-337 | 12 | |
| α-helix | 338-340 | 3 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-348 | 3 | |
| α-helix | 349-353 | 5 | |
| α-helix | 358-376 | 19 | |
| α-helix | 378-388 | 11 | |
| α-helix | 390-393 | 4 | |
| α-helix | 396-399 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lactose permease | A, B | protein | 417 | ESCHERICHIA COLI | P02920 (AlphaFold model) |
>2V8N_1 LACTOSE PERMEASE (chains A, B) MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQ PLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNA GAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALIL AVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD QQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMS VRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQL AMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA
Structural Determination of Wild-Type Lactose Permease. Guan, L., Mirza, O., Verner, G. et al. Proc Natl Acad Sci U S A (2007) 104:15294. DOI 10.1073/PNAS.0707688104 · 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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