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{
"metadata": {
"accession": "IPR013154",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF08240": "Alcohol dehydrogenase GroES-like domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR013154",
"name": "Alcohol dehydrogenase-like, N-terminal",
"type": "Domain",
"children": []
},
"name": {
"name": "Alcohol dehydrogenase-like, N-terminal",
"short": "ADH-like_N"
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{
"text": "<p>This is the catalytic domain of alcohol dehydrogenases ([ec:1.1.1.1]). Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure; a name derived from the superfamily of proteins with a GroES fold. Proteins with a GroES fold structure have a highly conserved hydrophobic core and a glycyl-aspartate dipeptide which is thought to maintain the fold [[cite:PUB00017153], [cite:PUB00015341]].</p>",
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"literature": {
"PUB00015341": {
"PMID": 8804825,
"ISBN": null,
"volume": "6",
"issue": "3",
"year": 1996,
"title": "Structural classification of proteins: new superfamilies.",
"URL": null,
"raw_pages": "386-94",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Murzin AG."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0959-440X(96)80059-5"
},
"PUB00017153": {
"PMID": 10556240,
"ISBN": null,
"volume": "12",
"issue": "10",
"year": 1999,
"title": "Conserved structural features and sequence patterns in the GroES fold family.",
"URL": null,
"raw_pages": "815-8",
"medline_journal": "Protein Eng",
"ISO_journal": "Protein Eng.",
"authors": [
"Taneja B",
"Mande SC."
],
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}
},
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"accession": "IPR011032",
"name": "GroES-like superfamily",
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],
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"interactions": 0,
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"pathways": 564,
"proteins": 537162,
"proteomes": 11525,
"sets": 0,
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},
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"taxa": 46155
},
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"alignment:full": 171194
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}