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Protein Overview: PYRB_ECOLI

General Information:
Name(s) found: PYRB_ECOLI [Swiss-Prot]
Description(s) found:
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  • gi|88192068|pdb|2AIR|G Chain G, T-State Active Site Of Aspartate Transcarbamylase:crystal Structure Of The Carbamyl Phosphate And L-Alanosine Ligated Enzyme [NCBI NR]
  • gi|88192066|pdb|2AIR|A Chain A, T-State Active Site Of Aspartate Transcarbamylase:crystal Structure Of The Carbamyl Phosphate And L-Alanosine Ligated Enzyme [NCBI NR]
  • gi|71042236|pdb|1ZA2|C Chain C, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp, Carbamoyl Phosphate At 2.50 A Resolution [NCBI NR]
  • gi|71042234|pdb|1ZA2|A Chain A, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp, Carbamoyl Phosphate At 2.50 A Resolution [NCBI NR]
  • gi|71042232|pdb|1ZA1|C Chain C, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp At 2.20 A Resolution [NCBI NR]
  • gi|71042230|pdb|1ZA1|A Chain A, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp At 2.20 A Resolution [NCBI NR]
  • gi|5107741|pdb|3CSU|C Chain C, Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase [NCBI NR]
  • gi|5107740|pdb|3CSU|B Chain B, Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase [NCBI NR]
  • gi|5107739|pdb|3CSU|A Chain A, Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase [NCBI NR]
  • gi|494532|pdb|1RAI|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494530|pdb|1RAI|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494528|pdb|1RAH|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494526|pdb|1RAH|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494524|pdb|1RAG|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494522|pdb|1RAG|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494520|pdb|1RAF|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494518|pdb|1RAF|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494516|pdb|1RAE|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494514|pdb|1RAE|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494512|pdb|1RAD|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494510|pdb|1RAD|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494508|pdb|1RAC|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494506|pdb|1RAC|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494504|pdb|1RAB|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494502|pdb|1RAB|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494500|pdb|1RAA|C Chain C, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|494498|pdb|1RAA|A Chain A, Crystal Structure Of Ctp-Ligated T State Aspartate Transcarbamoylase At 2.5 Angstroms Resolution: Implications For Atcase Mutants And The Mechanism Of Negative Cooperativity [NCBI NR]
  • gi|49258619|pdb|1R0C|G Chain G, Products In The T State Of Aspartate Transcarbamylase: Crystal Structure Of The Phosphate And N-Carbamyl-L- Aspartate Ligated Enzyme [NCBI NR]
  • gi|49258617|pdb|1R0C|A Chain A, Products In The T State Of Aspartate Transcarbamylase: Crystal Structure Of The Phosphate And N-Carbamyl-L- Aspartate Ligated Enzyme [NCBI NR]
  • gi|49258613|pdb|1R0B|F Chain F, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258612|pdb|1R0B|E Chain E, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258611|pdb|1R0B|D Chain D, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258607|pdb|1R0B|C Chain C, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258606|pdb|1R0B|B Chain B, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258605|pdb|1R0B|A Chain A, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258575|pdb|1Q95|F Chain F, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258574|pdb|1Q95|E Chain E, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258573|pdb|1Q95|D Chain D, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258572|pdb|1Q95|C Chain C, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258571|pdb|1Q95|B Chain B, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|49258570|pdb|1Q95|A Chain A, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [NCBI NR]
  • gi|194709188|pdb|3D7S|C Chain C, Crystal Structure Of Wild-Type E. Coli Asparate Transcarbamoylase At Ph 8.5 At 2.80 A Resolution [NCBI NR]
  • gi|194709186|pdb|3D7S|A Chain A, Crystal Structure Of Wild-Type E. Coli Asparate Transcarbamoylase At Ph 8.5 At 2.80 A Resolution [NCBI NR]
  • gi|168177080|pdb|2QGF|C Chain C, Structure Of Regulatory Chain Mutant H20a Of Asparate Transcarbamoylase From E. Coli [NCBI NR]
  • gi|168177078|pdb|2QGF|A Chain A, Structure Of Regulatory Chain Mutant H20a Of Asparate Transcarbamoylase From E. Coli [NCBI NR]
  • gi|168177076|pdb|2QG9|C Chain C, Structure Of A Regulatory Subunit Mutant D19a Of Atcase From E. Coli [NCBI NR]
  • gi|168177074|pdb|2QG9|A Chain A, Structure Of A Regulatory Subunit Mutant D19a Of Atcase From E. Coli [NCBI NR]
  • gi|158428832|pdb|2IPO|C Chain C, E. Coli Aspartate Transcarbamoylase Complexed With N- Phosphonacetyl-L-Asparagine [NCBI NR]
  • gi|158428830|pdb|2IPO|A Chain A, E. Coli Aspartate Transcarbamoylase Complexed With N- Phosphonacetyl-L-Asparagine [NCBI NR]
  • gi|118137861|pdb|2H3E|C Chain C, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of N-Phosphonacetyl-L-Isoasparagine At 2.3a Resolution [NCBI NR]
  • gi|118137859|pdb|2H3E|A Chain A, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of N-Phosphonacetyl-L-Isoasparagine At 2.3a Resolution [NCBI NR]
  • gi|114793926|pdb|2FZK|C Chain C, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.50 Resolution [NCBI NR]
  • gi|114793924|pdb|2FZK|A Chain A, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.50 Resolution [NCBI NR]
  • gi|114793922|pdb|2FZG|C Chain C, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.25 Resolution [NCBI NR]
  • gi|114793920|pdb|2FZG|A Chain A, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.25 Resolution [NCBI NR]
  • gi|114793918|pdb|2FZC|C Chain C, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.10 Resolution [NCBI NR]
  • gi|114793916|pdb|2FZC|A Chain A, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.10 Resolution [NCBI NR]
  • (P0A786) Aspartate carbamoyltransferase catalytic chain (EC 2.1.3.2) (Aspartate transcarbamylase) (ATCase) [Swiss-Prot]
  • Chain G, Products In The T State Of Aspartate Transcarbamylase: Crystal Structure Of The Phosphate And N-Carbamyl-L- Aspartate Ligated Enzymegi|49258617|pdb|1R0C|A Chain A, Products In The T State Of Aspartate Transcarbamylase: Crystal Structure Of The P [nrdb_11152004_Chlamydomonas]
  • Chain F, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [nr-271106-contam.fasta]
  • Chain A, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.25 Resolution [nr-271106-contam.fasta]
  • Chain B, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [nr-271106-contam.fasta]
  • Chain C, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.10 Resolution [nr-271106-contam.fasta]
  • Chain G, T-State Active Site Of Aspartate Transcarbamylase:crystal Structure Of The Carbamyl Phosphate And L-Alanosine Ligated Enzyme [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Fast Cooling Sa Refinement After 500 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [nr-271106-contam.fasta]
  • Chain E, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [nr-271106-contam.fasta]
  • Chain D, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Slow Cooling Sa Refinement After 1000 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Fast Cooling Sa Refinement After 500 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Slow Cooling Sa Refinement After 750 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Fast Cooling Sa Refinement After 1000 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain C, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.50 Resolution [nr-271106-contam.fasta]
  • Chain A, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp, Carbamoyl Phosphate At 2.50 A Resolution [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Fast Cooling Sa Refinement After 1000 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.50 Resolution [nr-271106-contam.fasta]
  • Chain C, Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Slow Cooling Sa Refinement After 1000 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp At 2.20 A Resolution [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Slow Cooling Sa Refinement After 750 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Fast Cooling Sa Refinement After 250 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Fast Cooling Sa Refinement After 250 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain G, Products In The T State Of Aspartate Transcarbamylase: Crystal Structure Of The Phosphate And N-Carbamyl-L- Aspartate Ligated Enzyme [nr-271106-contam.fasta]
  • Chain A, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of N-Phosphonacetyl-L-Isoasparagine At 2.3a Resolution [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Refinement 9: Final Refined Structure) [nr-271106-contam.fasta]
  • Chain C, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.25 Resolution [nr-271106-contam.fasta]
  • Chain C, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of N-Phosphonacetyl-L-Isoasparagine At 2.3a Resolution [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamylase (Atcase) Of Escherichia Coli: A New Crystalline R State Bound To Pala, Or To Product Analogues Phosphate And Citrate [nr-271106-contam.fasta]
  • Chain B, Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Fast Cooling Sa Refinement After 750 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Slow Cooling Sa Refinement After 500 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Refinement 9: Final Refined Structure) [nr-271106-contam.fasta]
  • Chain C, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp, Carbamoyl Phosphate At 2.50 A Resolution [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Fast Cooling Sa Refinement After 750 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, T-State Active Site Of Aspartate Transcarbamylase:crystal Structure Of The Carbamyl Phosphate And L-Alanosine Ligated Enzyme [nr-271106-contam.fasta]
  • Chain A, Products In The T State Of Aspartate Transcarbamylase: Crystal Structure Of The Phosphate And N-Carbamyl-L- Aspartate Ligated Enzyme [nr-271106-contam.fasta]
  • Chain C, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Slow Cooling Sa Refinement After 250 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Slow Cooling Sa Refinement After 500 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain A, Catalytic Trimer Of Escherichia Coli Aspartate Transcarbamoylase [nr-271106-contam.fasta]
  • Chain A, Aspartate Transcarbamoylase (E.C.2.1.3.2) (Aspartate Carbamoyltransferase) (T State) Complexed With Ctp (Slow Cooling Sa Refinement After 250 Steps Of Equilibration Of Preliminary Refined Model) [nr-271106-contam.fasta]
  • Chain C, Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In The Presence Of Ctp At 2.20 A Resolution [nr-271106-contam.fasta]
  • Chain A, The Structure Of Wild-Type E. Coli Aspartate Transcarbamoylase In Complex With Novel T State Inhibitors At 2.10 Resolution [nr-271106-contam.fasta]
    • Organism: Escherichia coli
    Length: 310 amino acids

    Gene Ontology:
    Cellular Component: NONE FOUND
    Biological Process: NONE FOUND
    Molecular Function: NONE FOUND


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 ANPLYQKHII SINDLSRDDL NLVLATAAKL KANPQPELLK HKVIASCFFE ASTRTRLSFE  60
   61 TSMHRLGASV VGFSDSANTS LGKKGETLAD TISVISTYVD AIVMRHPQEG AARLATEFSG 120
  121 NVPVLNAGDG SNQHPTQTLL DLFTIQETQG RLDNLHVAMV GDLKYGRTVH SLTQALAKFD 180
  181 GNRFYFIAPD ALAMPQYILD MLDEKGIAWS LHSSIEEVMA EVDILYMTRV QKERLDPSEY 240
  241 ANVKAQFVLR ASDLHNAKAN MKVLHPLPRV DEIATDVDKT PHAWYFQQAG NGIFARQALL 300
  301 ALVLNRDLVL

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Noble WS, et al. (2009) Manuscript in preparation. PYRB_ECOLI gi|134105085, gi... gi|189095939, gi...

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    SHOWING SINGLE HITS. [ Hide Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

    New Feature: Upload Your Own Microscopy Data

    No microscopy data found in the PDR for this protein.

    Protein Structure Data



    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.99

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle