Crystal structure of E. coli Lactose permease G46W/G262W bound to p-nitrophenyl alpha-D-galactopyranoside (alpha-NPG). Determined by X-ray diffraction at 3.31 Å resolution. Released 29 Jul 2015.
Explore 4ZYR in 3D Show helices and sheets RCSB PDB PDBe
4ZYR 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 | 45-52 | 8 | |
| α-helix | 60-69 | 10 | |
| α-helix | 75-83 | 9 | |
| α-helix | 84-86 | 3 | |
| α-helix | 87-90 | 4 | |
| α-helix | 91-95 | 5 | |
| α-helix | 96-101 | 6 | |
| α-helix | 108-111 | 4 | |
| α-helix | 112-114 | 3 | |
| α-helix | 115-119 | 5 | |
| α-helix | 122-132 | 11 | |
| α-helix | 141-160 | 20 | |
| α-helix | 168-186 | 19 | |
| α-helix | 210-213 | 4 | |
| 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 | 288-305 | 18 | |
| α-helix | 306-308 | 3 | |
| α-helix | 312-340 | 29 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-351 | 6 | |
| α-helix | 352-356 | 5 | |
| α-helix | 357-361 | 5 | |
| α-helix | 364-376 | 13 | |
| α-helix | 378-395 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-24 | 18 | |
| α-helix | 30-35 | 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 | 90-95 | 6 | |
| α-helix | 96-100 | 5 | |
| α-helix | 105-108 | 4 | |
| α-helix | 112-114 | 3 | |
| α-helix | 115-119 | 5 | |
| α-helix | 122-132 | 11 | |
| α-helix | 140-160 | 21 | |
| α-helix | 168-186 | 19 | |
| α-helix | 210-213 | 4 | |
| 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 | 288-305 | 18 | |
| α-helix | 312-340 | 29 | |
| α-helix | 343-345 | 3 | |
| α-helix | 346-351 | 6 | |
| α-helix | 352-357 | 6 | |
| α-helix | 358-373 | 16 | |
| α-helix | 378-399 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lactose permease | A, B | protein | 417 | Escherichia coli (strain K12) | P02920 (AlphaFold model) |
>4ZYR_1 Lactose permease (chains A, B) MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTWIIFAAISLFSLLFQ PLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNA GAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALCASIVGIMFTINNQFVFWLGSGCALIL AVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD QQFANFFTSFFATGEQGTRVFWYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMS VRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQL AMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA
| ID | Name | Formula | Copies |
|---|---|---|---|
| 9PG | 4-nitrophenyl alpha-D-galactopyranoside | C12 H15 N O8 | 2 |
| BNG | nonyl beta-D-glucopyranoside | C15 H30 O6 | 2 |
Structure of LacY with an alpha-substituted galactoside: Connecting the binding site to the protonation site. Kumar, H., Finer-Moore, J.S., Kaback, H.R. et al. Proc Natl Acad Sci U S A (2015) 112:9004-9009. DOI 10.1073/pnas.1509854112 · 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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