Transcriptional activator 3D structures

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3D Structures of transcriptional activator3D Structures of transcriptional activator

Updated on 01-January-2024 - For a general description of the protein see Transcriptional activator

  • BgaR TA
  • SlyA TA
    • 1lj9 – EfTA
    • 3qpt – StTA
    • 3q5f – StTA + DNA
    • 4aih – YpTA – Yersinia pseudotuberculosis
    • 4aij, 4aik – YpTA + DNA
  • CouR TA
    • 5cyv, 6c28 – RjTA + coumaroyl-CoA – Rhodococcus jostii
    • 6c9t – RpTA
    • 6c2s – RpTA + DNA
  • CueR TA
  • LuxR TA
  • LuxT TA
  • ClgR TA or Clp gene regulator
  • LmrR TA
    • 3f8b, 6i8n – LlTA – Lactococcus lactis
    • 3f8c, 3f8f – LlTA + drug
    • 6vwe, 6do0 – LlTA + Rh complex
    • 6r1l – LlTA + Cu + phenanthroline
    • 4zzd – LlTA + riboflavine
    • 6fuu – LlTA + heme
  • MvfR TA
  • HdfR TA
    • 6wn5 – TA – Klebsiella pneumoniae
  • McbR TA
  • MetR TA
  • YvhJ TA
  • CgmR TA
  • AraR TA or arabinose metabolism transcriptional repressor
    • 5bs6, 5dd4 – BtTA – Bacterioides thetaiotaomicron
    • 3tb6 – BtTA effector-binding domain 71-362 + arabinose
    • 5ddg – BtTA + DNA
    • 5deq – BtTA 1-225 + arabinose
    • 4egy, 4egz, 4h0e, 5d4r, 5d4s – BsTA DBD 1-68 + DNA
  • CarH TA or light-dependent transcriptional regulator
  • ZitR TA or zinc transport transcriptional regulator
  • LsrR TA
  • TA II
    • 8igr – EcTA in transcription activation complex – Cryo EM
  • TA RAMA
    • 7bef, 7beg – EcTA in transcription activation complex – Cryo EM
  • PrfA TA or listeriolysin positive regulatory factor A
  • HTH-type TA or helix-turn-helix-type
    • 2uxu – PpTA TtgR + naringenin
    • 2uxh – PpTA TtgR + quercetin
    • 2uxi – PpTA TtgR + phloretin
    • 6ugl, 6kju – VcTA + pyrazine derivative<br />
    • 2bv6 – SaTA MgrA – Staphylococcus aureus
    • 5hs5, 5ywj, 6k8e – SaTA SarX
    • 3hrm, 3hse – SaTA SarZ
    • 6r1p – MtTA EthR
    • 1ysq – EcTA YiaJ
    • 2qop, 3bcg – EcTA AcrR
    • 6ldi, 6xh7, 6xh8, 7c17 – EcTA CueR in transcription activation complex – Cryo EM
    • 4wls, 4wlw – EcTA CueR + DNA
    • 4x1e – EcTA RutR
    • 4xk4, 4jyk – EcTA RutR + uracil derivative
    • 2hxr – EcTA CynR LBD
    • 3hfu – EcTA CynR LBD + N3
    • 8bob – EcTA MalT + MalY – Cryo EM
    • 2gfn – RjTA Rha1
    • 1i1g – PfTA LrpA
    • 7cla – TA SkgA – Caulobacter vibrioides
    • 7bzd – BsTA HxlR
    • 7bze – BsTA HxlR (mutant)
    • 7bzg – BsTA HxlR + DNA
    • 7amn, 7amt – TA LuxR + DNA – Vibrio alginolyticus
    • 2dtz, 2hq5 – SaTA QacR (mutant)
    • 3bqz, 3br0, 3btc, 3btl – SaTA QacR (mutant) + malachite green
    • 3br1, 3br2, 3bt9, 3btj – SaTA QacR (mutant) + dequalinium
    • 3bti – SaTA QacR (mutant) + berberine
    • 1qvu,3br3, 3pm1 – SaTA QacR (mutant) + ethidium
    • 1rkw, 1rpw – SaTA QacR (mutant) + pentamadine
    • 1qvt – SaTA QacR (mutant) + proflavine
    • 3br5, 3br6 – SaTA QacR (mutant) + rhodamine
    • 2gby – SaTA QacR (mutant) + berenil
    • 2g0e – SaTA QacR (mutant) + drug
    • 3k1n – AbTA BenM – Acinetobacter baylyi
    • 3k1p – AbTA BenM (mutant)
    • 2f6g, 2f6p, 2f97 – AbTA BenM effector-binding domain 81-304
    • 3m1e – AbTA BenM DBD 1-87
    • 4ihs, 4iht – AbTA BenM effector-binding domain + DNA
    • 2f78, 2f7a, 2f7c – AbTA BenM effector-binding domain + effector
    • 2h9b – EfTA BenM (mutant)
    • 2f7b, 2h98 – AbTA CatM effector-binding domain
    • 3glb – AbTA CatM effector-binding domain (mutant)
    • 2f7c – AbTA CatM effector-binding domain + muconate
    • 2cfx – BsTA LrpC
    • 2gqq – EcTA LrpC
    • 6d2s, 6cyj, 6cz6, 6cyy – MtTA PrpR
    • 2pju – EcTA PrpR
    • 5t4k, 5t4j, 5t4l, 5x03 – BsTA GabR EBO domain + pyridine derivative
    • 4mgr, 4nob, 4tv7 – BsTA GabR
    • 6uxz – BsTA GabR + agonist
    • 5u9e, 5u93 – TA RhaR regulatory domain – Bacteria latreille
    • 5z49 – TA CmpR effector-binding domain + ribulose bisphosphate – Synechococcus elongatus
    • 3kos – CfTA AmpR effector binding domain – Citrobacter freundii
    • 3kot – CfTA AmpR effector binding domain (mutant)
    • 4wkm – CfTA AmpR effector binding domain + peptide
    • 5mmh – PaTA AmpR effector binding domain

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Michal Harel, Joel L. Sussman