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Crystal structure of tm0922, a fusion of a domain of unknown function and ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Thermotoga maritima soaked with Acetyl Coenzyme A
Biology and Chemistry Report
3RTA
  •   Structure Details   Hide

    Structure Keywords

    Keywords LYASE
    Text Unknown function, ADP/ATP-dependent NAD(P)H-hydrate dehydratase, LYASE

    Polymeric Molecules

    Chain A
    Description Putative uncharacterized protein 
    Nonstandard Linkage no 
    Nonstandard Monomers no 
    Polymer Type polypeptide(L) 
    Formula Weight 54528.3 
    Source Method genetically manipulated  
    Chain B
    Description Unknown peptide, probably from expression host 
    Nonstandard Linkage no 
    Nonstandard Monomers no 
    Polymer Type polypeptide(L) 
    Formula Weight 806.9 
    Source Method natural source  

    Ligands and Prosthetic Groups

    ID Name Chemical Formula Weight Ligand Structure
    ACO  ACETYL COENZYME *A  C23 H38 N7 O17 P3 S   809.57  View 
    POTASSIUM ION  K   39.10  View 
     
  •   Protein Details   Hide

    UniProtKB Information

    Chain SWS/UNP ID SWS/UNP Accession(s)
    A NNR_THEMA Q9X024     

    Keywords and Names

    Chain(s) RCSB Name UniProtKB Name UniProtKB Keywords

    EC, Associated Pathways and Catalytic Sites

    Chain(s) IUBMB KEGG BioCyc
    4.2.1.93      
    C: Cellular Location | F: Molecular Function | P: Biological Process
    Chain A
    GO ID   Ontology GO Term Definition
    8152   Metabolic Process  The Chemical Reactions and Pathways Including Anabolism and Catabolism by Which Living Organisms Transform Chemical Substances. Metabolic Processes Typically Transform Small Molecules But Also Include Macromolecular Processes Such As DNA Repair and Replication and Protein Synthesis and Degradation. 
    166   Nucleotide Binding  Interacting Selectively and Non Covalently with a Nucleotide Any Compound Consisting of a Nucleoside That Is Esterified with (ortho)phosphate or an Oligophosphate At Any Hydroxyl Group On the Ribose or Deoxyribose. 
    3824   Catalytic Activity  Catalysis of a Biochemical Reaction At Physiological Temperatures. in Biologically Catalyzed Reactions the Reactants Are Known As Substrates and the Catalysts Are Naturally Occurring Macromolecular Substances Known As Enzymes. Enzymes Possess Specific Binding Sites For Substrates and Are Usually Composed Wholly or Largely of Protein But RNA That Has Catalytic Activity (ribozyme) Is Often Also Regarded As Enzymatic. 
    5524   ATP Binding  Interacting Selectively and Non Covalently with ATP Adenosine 5' Triphosphate a Universally Important Coenzyme and Enzyme Regulator. 
    16829   Lyase Activity  Catalysis of the Cleavage of C C C O C N and Other Bonds by Other Means Than by Hydrolysis or Oxidation or Conversely Adding a Group to a Double Bond. They Differ From Other Enzymes in That Two Substrates Are Involved in One Reaction Direction But Only One in the Other Direction. When Acting On the Single Substrate a Molecule Is Eliminated and This Generates Either a New Double Bond or a New Ring. 
    16853   Isomerase Activity  Catalysis of the Geometric or Structural Changes Within One Molecule. Isomerase Is the Systematic Name For Any Enzyme of EC Class 5. 
    46872   Metal Ion Binding  Interacting Selectively and Non Covalently with Any Metal Ion. 


     
  •   Gene Details   Hide

    Natural Source

    Chain B
    Scientific Name Escherichia coli  
    Strain BL21(DE3)
    Details Unknown Peptide Probably From Expression Host

    Genetic Source

    Chain A
    Scientific Name Thermotoga maritima  
    Genus Thermotoga
    Species Thermotoga Maritima
    Strain MSB8
    Gene tm0922, tm_0922
    Host Scientific Name Escherichia coli  
    Host Strain Bl21(de3)
    Host Vector Type Plasmid
    Host Plasmid Name pMH1


    Genome Information

    Chromosome Locus Gene ID Gene Name Symbol
    - - 898596     hypothetical protein TM0922