4RZT: Lac repressor

Lac repressor engineered to bind sucralose, sucralose-bound tetramer. Determined by X-ray diffraction at 3.1 Å resolution. Released 23 Dec 2015.

Method
X-ray diffraction
Resolution
3.1 Å
Organism
Escherichia coli
Chains
4
Atoms
8,787
Mol. weight
165.12 kDa
Released
23 Dec 2015

Explore 4RZT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4RZT contains 44 α-helices and 68 β-strands across 4 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: 10 helices, 17 β-strands

ElementResiduesLengthSheet
β-strand63-6971
α-helix74-9017
β-strand93-9971
α-helix103-11614
β-strand122-12541
α-helix130-13910
β-strand145-14731
β-strand15811
β-strand160-16122
α-helix163-17715
β-strand182-18653
α-helix192-20615
β-strand214-21743
α-helix222-23413
β-strand241-24443
α-helix247-25913
β-strand26414
β-strand26814
β-strand269-27133
β-strand27415
α-helix277-2815
β-strand28713
β-strand288-29035
α-helix293-30816
β-strand318-31922
β-strand322-32435
α-helix339-35921
Chain B: 12 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand63-6971
α-helix74-9017
β-strand93-9971
α-helix103-11614
β-strand122-12541
α-helix130-13910
β-strand145-14731
β-strand15811
β-strand160-16126
α-helix163-17715
β-strand182-18657
α-helix192-20615
β-strand214-21747
α-helix222-23413
β-strand241-24447
α-helix247-25913
β-strand26418
β-strand26818
β-strand269-27137
β-strand27419
α-helix277-2815
α-helix285-2862
β-strand28717
β-strand288-29039
α-helix293-30816
β-strand318-31926
β-strand322-32439
α-helix339-35214
α-helix353-3553
Chain C: 11 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand63-69710
α-helix74-9017
β-strand93-99710
α-helix103-11614
β-strand122-125410
α-helix130-13910
β-strand145-147310
β-strand158110
β-strand160-161211
α-helix163-17715
β-strand182-186512
α-helix192-20615
β-strand214-217412
α-helix222-23413
β-strand241-244412
α-helix247-25913
β-strand264113
β-strand268113
β-strand269-271312
β-strand274114
α-helix277-2815
α-helix285-2862
β-strand287112
β-strand288-290314
α-helix293-30816
β-strand318-319211
β-strand322-324314
α-helix339-35921
Chain D: 11 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand63-69710
α-helix74-9017
β-strand93-99710
α-helix103-11614
β-strand122-125410
α-helix130-13910
β-strand145-147310
β-strand158110
β-strand160-161215
α-helix163-17715
β-strand182-186516
α-helix192-20615
β-strand214-217416
α-helix222-23413
β-strand241-244416
α-helix247-25913
β-strand264117
β-strand268117
β-strand269-271316
β-strand274118
α-helix277-2815
α-helix285-2862
β-strand287116
β-strand288-290318
α-helix293-30816
β-strand318-319215
β-strand322-324318
α-helix339-35517

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lac repressorA, B, C, Dprotein381Escherichia coliP03023 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4RZT_1 Lac repressor (chains A, B, C, D)
MGSSHHHHHHSSGLVPRGSHMVKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVE
AAMAELNYIPNRVAQQLAGKQSLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMV
ERSGVEACKAAVHNLLAQRVSGLIINYPLDDQDAIAVEAACTNVPALFLTASDQTPLNSI
IFSHEDGTRLGVEHLVALGHQQIALLAGPLSSVDARLRLAGWHKYLTRNQIQPIAEREGD
WSAMSGFQQTMQMLNEGIVPTAMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDS
SCYIPPLTTIKQDFRLLGQTSVDRLLQLSQGQAVKGNQLLPVSLVKRKTTLAPNTQTASP
RALADSLMQLARQVSRLESGQ

Primary citation

Engineering an allosteric transcription factor to respond to new ligands. Taylor, N.D., Garruss, A.S., Moretti, R. et al. Nat Methods (2016) 13:177-183. DOI 10.1038/nmeth.3696 · PubMed

Other PDB entries of the same protein (UniProt P03023 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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