Sugar Free Lactose Permease at neutral pH. Determined by X-ray diffraction at 2.95 Å resolution. Released 13 Mar 2006.
Explore 2CFQ in 3D Show helices and sheets RCSB PDB PDBe
2CFQ contains 33 α-helices and 0 β-strands across 1 chain. 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 | 30-31 | 2 | |
| α-helix | 32-38 | 7 | |
| α-helix | 46-67 | 22 | |
| α-helix | 75-82 | 8 | |
| α-helix | 87-90 | 4 | |
| α-helix | 91-95 | 5 | |
| α-helix | 96-100 | 5 | |
| α-helix | 105-108 | 4 | |
| α-helix | 109-111 | 3 | |
| α-helix | 116-119 | 4 | |
| α-helix | 122-136 | 15 | |
| α-helix | 140-143 | 4 | |
| α-helix | 150-164 | 15 | |
| α-helix | 167-170 | 4 | |
| α-helix | 180-183 | 4 | |
| α-helix | 210-216 | 7 | |
| α-helix | 220-228 | 9 | |
| α-helix | 229-234 | 6 | |
| α-helix | 235-249 | 15 | |
| α-helix | 254-257 | 4 | |
| α-helix | 259-268 | 10 | |
| α-helix | 269-273 | 5 | |
| α-helix | 274-286 | 13 | |
| α-helix | 288-306 | 19 | |
| α-helix | 312-318 | 7 | |
| α-helix | 321-340 | 20 | |
| α-helix | 343-349 | 7 | |
| α-helix | 350-357 | 8 | |
| α-helix | 358-365 | 8 | |
| α-helix | 367-370 | 4 | |
| α-helix | 372-375 | 4 | |
| α-helix | 377-396 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lactose permease | A | protein | 417 | ESCHERICHIA COLI | P02920 (AlphaFold model) |
>2CFQ_1 LACTOSE PERMEASE (chains A) MYYLKNTNFWMFGLFFFFYFFIMGAYFPFFPIWLHDINHISKSDTGIIFAAISLFSLLFQ PLFGLLSDKLGLRKYLLWIITGMLVMFAPFFIFIFGPLLQYNILVGSIVGGIYLGFCFNA GAPAVEAFIEKVSRRSNFEFGRARMFGCVGWALGASIVGIMFTINNQFVFWLGSGCALIL AVLLFFAKTDAPSSATVANAVGANHSAFSLKLALELFRQPKLWFLSLYVIGVSCTYDVFD QQFANFFTSFFATGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMS VRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSATIYLVCFCFFKQL AMIFMSVLAGNMYESIGFQGAYLVLGLVALGFTLISVFTLSGPGPLSLLRRQVNEVA
| ID | Name | Formula | Copies |
|---|---|---|---|
| HG | Mercury (II) ion | Hg | 5 |
Structural Evidence for Induced Fit and a Mechanism for Sugar/H(+) Symport in Lacy. Mirza, O., Guan, L., Verner, G. et al. EMBO J (2006) 25:2038. DOI 10.1038/SJ.EMBOJ.7601028 · 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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