1EFA: Lac repressor dimer

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.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Escherichia coli
Chains
5
Atoms
7,838
Mol. weight
121.05 kDa
Ligands
NPF
Released
6 Mar 2000

Explore 1EFA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 14 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix6-116
α-helix17-248
α-helix33-4513
α-helix51-566
β-strand63-6861
α-helix74-8916
β-strand93-9861
α-helix104-11613
β-strand121-12551
α-helix130-13910
β-strand145-14731
β-strand158-16141
α-helix163-17614
β-strand182-18652
α-helix192-20615
β-strand214-21742
α-helix222-23413
β-strand241-24442
α-helix247-25812
α-helix262-2632
β-strand26413
β-strand26813
β-strand269-27132
β-strand272-27434
α-helix277-2815
β-strand288-29034
α-helix293-30816
β-strand316-31941
β-strand322-32434
Chain B: 14 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix6-116
α-helix17-248
α-helix33-4412
α-helix51-566
β-strand63-6975
α-helix74-8916
β-strand93-9975
α-helix104-11613
β-strand121-12555
α-helix130-13910
β-strand145-14735
β-strand158-16145
α-helix163-17614
β-strand182-18656
α-helix192-20615
β-strand214-21746
α-helix222-23413
β-strand241-24446
α-helix247-25812
α-helix262-2632
β-strand26417
β-strand26817
β-strand269-27466
α-helix278-2814
β-strand287-29046
α-helix293-30816
β-strand316-31945
β-strand322-32436
Chain C: 11 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix51-566
β-strand63-6978
α-helix74-8916
β-strand93-9978
α-helix104-11613
β-strand121-12558
α-helix130-13910
β-strand145-14738
β-strand158-16148
α-helix163-17614
β-strand182-18659
α-helix192-20615
β-strand214-21749
α-helix222-23413
β-strand241-24449
α-helix247-25812
α-helix262-2632
β-strand264110
β-strand268110
β-strand269-27469
α-helix278-2814
β-strand287-29049
α-helix293-30816
β-strand316-31948
β-strand322-32439

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
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, EDNA21
Lac repressorA, B, Cprotein333Escherichia coliP03023 (AlphaFold model)
Sequence of entity 1 (D, E), FASTA
>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
Sequence of entity 2 (A, B, C), FASTA
>1EFA_2 LAC REPRESSOR (chains A, B, C)
MKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVEAAMAELNYIPNRVAQQLAGKQ
SLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMVERSGVEACKTAVHNLLAQRVS
GLIINYPLDDQDAIAVEAACTNVPALFLDVSDQTPINSIIFSHEDGTRLGVEHLVALGHQ
QIALLAGPLSSVSARLRLAGWHKYLTRNQIQPIAEREGDWSAMSGFQQTMQMLNEGIVPT
AMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDSSCYIPPLTTIKQDFRLLGQTS
VDRLLQLSQGQAVKGNQLLPVSLVKRKTTLAPN

Ligands and cofactors

IDNameFormulaCopies
NPF2-nitrophenyl beta-D-fucopyranosideC12 H15 N O73

Primary citation

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:

Browse more

1EFA is part of these collections:

About this viewer

MolViewer shows 1EFA directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.