{"entry": {"accession": "MF7000870", "general": {"name": "Human ALR, selenium substituted", "pdb_id": "3u5s", "exp_method": "X-ray", "resolution": "1.50", "assembly": "Homodimer", "source_organism": "Homo sapiens", "publication": {"pmid": "23159557", "authors": "Schaefer SA, Dong M, Rubenstein RP, Wilkie WA, Bahnson BJ, Thorpe C, Rozovsky S", "title": "(77)Se enrichment of proteins expands the biological NMR toolbox.", "journal": "J. Mol. Biol.", "year": "2013", "issue": "2", "volume": "425", "pages": "222-31", "abstract": "Sulfur, a key contributor to biological reactivity, is not amendable to investigations by biological NMR spectroscopy. To utilize selenium as a surrogate, we have developed a generally applicable (77)Se isotopic enrichment method for heterologous proteins expressed in Escherichia coli. We demonstrate (77)Se NMR spectroscopy of multiple selenocysteine and selenomethionine residues in the sulfhydryl oxidase augmenter of liver regeneration (ALR). The resonances of the active-site residues were assigned by comparing the NMR spectra of ALR bound to oxidized and reduced flavin adenine dinucleotide. An additional resonance appears only in the presence of the reducing agent and disappears readily upon exposure to air and subsequent reoxidation of the flavin. Hence, (77)Se NMR spectroscopy can be used to report the local electronic environment of reactive and structural sulfur sites, as well as changes taking place in those locations during catalysis."}}, "function": {"molecular_function": {"go": [{"accession": "GO:0050660", "name": "flavin adenine dinucleotide binding"}, {"accession": "GO:0016971", "name": "flavin-dependent sulfhydryl oxidase activity"}, {"accession": "GO:0008083", "name": "growth factor activity"}, {"accession": "GO:0015035", "name": "protein-disulfide reductase activity"}]}, "cellular_component": {"go": [{"accession": "GO:0005829", "name": "cytosol"}, {"accession": "GO:0005615", "name": "extracellular space"}, {"accession": "GO:0005758", "name": "mitochondrial intermembrane space"}, {"accession": "GO:0005739", "name": "mitochondrion"}]}, "biological_process": {"go": [{"accession": "GO:0072717", "name": "cellular response to actinomycin D"}, {"accession": "GO:0071222", "name": "cellular response to lipopolysaccharide"}, {"accession": "GO:0097237", "name": "cellular response to toxic substance"}, {"accession": "GO:0071356", "name": "cellular response to tumor necrosis factor"}, {"accession": "GO:0001889", "name": "liver development"}, {"accession": "GO:0097421", "name": "liver regeneration"}, {"accession": "GO:0043066", "name": "negative regulation of apoptotic process"}, {"accession": "GO:0045953", "name": "negative regulation of natural killer cell mediated cytotoxicity"}, {"accession": "GO:2000573", "name": "positive regulation of DNA biosynthetic process"}]}}, "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": "FAD-linked sulfhydryl oxidase ALR", "source_organism": "Homo sapiens", "uniprot": {"id": "P55789", "start": "82", "end": "205", "coverage": "60%", "sequence": "MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD", "length": "205"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "6", "region_end": "10"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "19", "region_end": "37"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "43", "region_end": "61"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "63", "region_end": "77"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "83", "region_end": "102"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "108", "region_end": "110"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "111", "region_end": "117"}, {"region_type": "pfam", "region_id": "PF04777", "region_name": "Erv1 / Alr family", "region_start": "104", "region_end": "196"}]}}, {"id": "A-2", "name": "FAD-linked sulfhydryl oxidase ALR", "source_organism": "Homo sapiens", "uniprot": {"id": "P55789", "start": "82", "end": "205", "coverage": "60%", "sequence": "MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD", "length": "205"}, "regions": {"region": {"region_type": "pfam", "region_id": "PF04777", "region_name": "Erv1 / Alr family", "region_start": "104", "region_end": "196"}}}]}, "evidence": {"evidence_level": "Insufficient evidence (candidate)", "evidence_coverage": "The full structure participates in mutual synergistic folding.", "sequence_domain": "ERV/ALR sulfhydryl oxidase domain", "complex_evidence": "There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface.", "chain_evidence": [{"chain_id": "A", "support": "N/A"}, {"chain_id": "A-2", "support": "N/A"}]}, "related_structures": {"id": ["MF7000866", "MF7000270", "MF7000867", "MF7000868", "MF7000869", "MF7000870"]}}}