{"entry": {"accession": "MF7000976", "general": {"name": "tRNA-specific adenosine deaminase (Streptococcus pyogenes)", "pdb_id": "2nx8", "exp_method": "X-ray", "resolution": "2.00", "assembly": "Homodimer", "source_organism": "Streptococcus pyogenes serotype M6", "publication": {"pmid": "17554781", "authors": "Lee WH, Kim YK, Nam KH, Priyadarshi A, Lee EH, Kim EE, Jeon YH, Cheong C, Hwang KY", "title": "Crystal structure of the tRNA-specific adenosine deaminase from Streptococcus pyogenes.", "journal": "Proteins", "year": "2007", "issue": "4", "volume": "68", "pages": "1016-9"}}, "function": {"molecular_function": {"go": [{"accession": "GO:0004131", "name": "cytosine deaminase activity"}, {"accession": "GO:0052717", "name": "tRNA-specific adenosine-34 deaminase activity"}, {"accession": "GO:0008270", "name": "zinc ion binding"}]}, "cellular_component": {"go": {"accession": "GO:0005737", "name": "cytoplasm"}}, "biological_process": {"go": [{"accession": "GO:0046087", "name": "cytidine metabolic process"}, {"accession": "GO:0019858", "name": "cytosine metabolic process"}, {"accession": "GO:0008655", "name": "pyrimidine-containing compound salvage"}, {"accession": "GO:0002100", "name": "tRNA wobble adenosine to inosine editing"}]}}, "macromolecules": {"general": {"nr_of_chains": "2", "nr_of_unique_protein_segments": "1", "class": "Homooligomeric enzymes", "subclass": "Homodimeric enzymes", "note": "All chains according to the most probable oligomerization state stored in PDBe were considered."}, "chain": [{"id": "A", "name": "tRNA-specific adenosine deaminase", "source_organism": "Streptococcus pyogenes serotype M6", "uniprot": {"id": "Q5XE14", "start": "1", "end": "165", "coverage": "96%", "sequence": "MPYSLEEQTYFMQEALKEAEKSLQKAEIPIGCVIVKDGEIIGRGHNAREESNQAIMHAEMMAINEANAHEGNWRLLDTTLFVTIEPCVMCSGAIGLARIPHVIYGASNQKFGGADSLYQILTDERLNHRVQVERGLLAADCANIMQTFFRQGRERKKIAKHLIKEQSDPFD", "length": "171"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "12", "region_end": "33"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "55", "region_end": "60"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "65", "region_end": "79"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "95", "region_end": "105"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "127", "region_end": "131"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "145", "region_end": "173"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "39", "region_end": "44"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "47", "region_end": "53"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "86", "region_end": "92"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "109", "region_end": "114"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "139", "region_end": "142"}, {"region_type": "pfam", "region_id": "PF14437", "region_name": "MafB19-like deaminase", "region_start": "7", "region_end": "153"}]}}, {"id": "A-2", "name": "tRNA-specific adenosine deaminase", "source_organism": "Streptococcus pyogenes serotype M6", "uniprot": {"id": "Q5XE14", "start": "1", "end": "165", "coverage": "96%", "sequence": "MPYSLEEQTYFMQEALKEAEKSLQKAEIPIGCVIVKDGEIIGRGHNAREESNQAIMHAEMMAINEANAHEGNWRLLDTTLFVTIEPCVMCSGAIGLARIPHVIYGASNQKFGGADSLYQILTDERLNHRVQVERGLLAADCANIMQTFFRQGRERKKIAKHLIKEQSDPFD", "length": "171"}, "regions": {"region": {"region_type": "pfam", "region_id": "PF14437", "region_name": "MafB19-like deaminase", "region_start": "7", "region_end": "153"}}}]}, "evidence": {"evidence_level": "Insufficient evidence (candidate)", "evidence_coverage": "The full structure participates in mutual synergistic folding.", "sequence_domain": "-", "complex_evidence": "The tRNA-specific adenosine deaminase, spTadA is a dimer in solution as demonstrated by gel-filtration. Dimer formation buries a large surface which is mainly formed by hydrophobic and nonpolar interactions. From the structural aspects, dimerization appears to be important for specific binding with tRNA and enzyme functions. The authors also suggest that because of the nonpolar interface, the formation of a dimer is energetically favorable compared with the monomer in solution. (PMID:17554781).", "chain_evidence": [{"chain_id": "A", "support": "N/A"}, {"chain_id": "A-2", "support": "N/A"}]}}}