Crystal structure of the lac repressor dimer bound to operator and the anti-inducer onpf. Determined by X-ray diffraction at 2.6 Å resolution. Released 6 Mar 2000.
Explore 1EFA in 3D Show helices and sheets RCSB PDB PDBe
1EFA contains 39 α-helices and 43 β-strands across 3 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 | 6-11 | 6 | |
| α-helix | 17-24 | 8 | |
| α-helix | 33-45 | 13 | |
| α-helix | 51-56 | 6 | |
| β-strand | 63-68 | 6 | 1 |
| α-helix | 74-89 | 16 | |
| β-strand | 93-98 | 6 | 1 |
| α-helix | 104-116 | 13 | |
| β-strand | 121-125 | 5 | 1 |
| α-helix | 130-139 | 10 | |
| β-strand | 145-147 | 3 | 1 |
| β-strand | 158-161 | 4 | 1 |
| α-helix | 163-176 | 14 | |
| β-strand | 182-186 | 5 | 2 |
| α-helix | 192-206 | 15 | |
| β-strand | 214-217 | 4 | 2 |
| α-helix | 222-234 | 13 | |
| β-strand | 241-244 | 4 | 2 |
| α-helix | 247-258 | 12 | |
| α-helix | 262-263 | 2 | |
| β-strand | 264 | 1 | 3 |
| β-strand | 268 | 1 | 3 |
| β-strand | 269-271 | 3 | 2 |
| β-strand | 272-274 | 3 | 4 |
| α-helix | 277-281 | 5 | |
| β-strand | 288-290 | 3 | 4 |
| α-helix | 293-308 | 16 | |
| β-strand | 316-319 | 4 | 1 |
| β-strand | 322-324 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-11 | 6 | |
| α-helix | 17-24 | 8 | |
| α-helix | 33-44 | 12 | |
| α-helix | 51-56 | 6 | |
| β-strand | 63-69 | 7 | 5 |
| α-helix | 74-89 | 16 | |
| β-strand | 93-99 | 7 | 5 |
| α-helix | 104-116 | 13 | |
| β-strand | 121-125 | 5 | 5 |
| α-helix | 130-139 | 10 | |
| β-strand | 145-147 | 3 | 5 |
| β-strand | 158-161 | 4 | 5 |
| α-helix | 163-176 | 14 | |
| β-strand | 182-186 | 5 | 6 |
| α-helix | 192-206 | 15 | |
| β-strand | 214-217 | 4 | 6 |
| α-helix | 222-234 | 13 | |
| β-strand | 241-244 | 4 | 6 |
| α-helix | 247-258 | 12 | |
| α-helix | 262-263 | 2 | |
| β-strand | 264 | 1 | 7 |
| β-strand | 268 | 1 | 7 |
| β-strand | 269-274 | 6 | 6 |
| α-helix | 278-281 | 4 | |
| β-strand | 287-290 | 4 | 6 |
| α-helix | 293-308 | 16 | |
| β-strand | 316-319 | 4 | 5 |
| β-strand | 322-324 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 51-56 | 6 | |
| β-strand | 63-69 | 7 | 8 |
| α-helix | 74-89 | 16 | |
| β-strand | 93-99 | 7 | 8 |
| α-helix | 104-116 | 13 | |
| β-strand | 121-125 | 5 | 8 |
| α-helix | 130-139 | 10 | |
| β-strand | 145-147 | 3 | 8 |
| β-strand | 158-161 | 4 | 8 |
| α-helix | 163-176 | 14 | |
| β-strand | 182-186 | 5 | 9 |
| α-helix | 192-206 | 15 | |
| β-strand | 214-217 | 4 | 9 |
| α-helix | 222-234 | 13 | |
| β-strand | 241-244 | 4 | 9 |
| α-helix | 247-258 | 12 | |
| α-helix | 262-263 | 2 | |
| β-strand | 264 | 1 | 10 |
| β-strand | 268 | 1 | 10 |
| β-strand | 269-274 | 6 | 9 |
| α-helix | 278-281 | 4 | |
| β-strand | 287-290 | 4 | 9 |
| α-helix | 293-308 | 16 | |
| β-strand | 316-319 | 4 | 8 |
| β-strand | 322-324 | 3 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA (5'-d(*gp*ap*ap*t*tp*gp*tp*gp*ap*gp*cp*gp*cp*tp*cp*ap*cp*ap*ap*tp*t)-3') | D, E | DNA | 21 | ||
| Lac repressor | A, B, C | protein | 333 | Escherichia coli | P03023 (AlphaFold model) |
>1EFA_1 DNA (5'-D(*GP*AP*AP*T*TP*GP*TP*GP*AP*GP*CP*GP*CP*TP*CP*AP*CP*AP*AP*TP*T)-3') (chains D, E) GAATTGTGAGCGCTCACAATT
>1EFA_2 LAC REPRESSOR (chains A, B, C) MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNRVAQQLAGKQ SLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMVERSGVEACKTAVHNLLAQRVS GLIINYPLDDQDAIAVEAACTNVPALFLDVSDQTPINSIIFSHEDGTRLGVEHLVALGHQ QIALLAGPLSSVSARLRLAGWHKYLTRNQIQPIAEREGDWSAMSGFQQTMQMLNEGIVPT AMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDSSCYIPPLTTIKQDFRLLGQTS VDRLLQLSQGQAVKGNQLLPVSLVKRKTTLAPN
| ID | Name | Formula | Copies |
|---|---|---|---|
| NPF | 2-nitrophenyl beta-D-fucopyranoside | C12 H15 N O7 | 3 |
A closer view of the conformation of the Lac repressor bound to operator. Bell, C.E., Lewis, M. Nat Struct Biol (2000) 7:209-214. DOI 10.1038/78907 · PubMed
Other PDB entries of the same protein (UniProt P03023 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1EFA is part of these collections:
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