p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

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  "angular_unit": "1/A",
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    "title": "Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.",
    "publication": {
      "title": "Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.",
      "author_list": "Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D",
      "journal": "Arch Biochem Biophys",
      "doi": "10.1016/j.abb.2018.06.010",
      "pmid": "29940152",
      "published_date": "2018 Sep 1"
    },
    "status": "released",
    "submitted_date": "2018-06-05",
    "released_date": "2018-06-29"
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      "name": "Synchrotron Light Research Institute (SLRI)",
      "city": "Nakhon Ratchasima",
      "country": "Thailand",
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          "long_name": "p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant",
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          "uniprot_code": "Q6Q271",
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        "affiliation": [
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            "short_name": null,
            "address": "Thailand",
            "full_name": "Mahidol University",
            "webpage": "https://mahidol.ac.th/"
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        "contributor_surname": "Yuenyao",
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