{"entry": {"accession": "MF7000866", "general": {"name": "Erv2p", "pdb_id": "1jr8", "exp_method": "X-ray", "resolution": "1.50", "assembly": "Homodimer", "source_organism": "Saccharomyces cerevisiae", "publication": {"pmid": "11740506", "authors": "Gross E, Sevier CS, Vala A, Kaiser CA, Fass D", "title": "A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.", "journal": "Nat. Struct. Biol.", "year": "2002", "issue": "1", "volume": "9", "pages": "61-7", "abstract": "Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum. The structure of Erv2p, determined by X-ray crystallography to 1.5 A resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The first (Cys-Gly-Glu-Cys) is adjacent to the isoalloxazine ring of the FAD. The second (Cys-Gly-Cys) is part of a flexible C-terminal segment that can swing into the vicinity of the first cysteine pair in the opposite subunit of the dimer and may shuttle electrons between substrate protein dithiols and the FAD-proximal disulfide."}}, "function": {"molecular_function": {"go": [{"accession": "GO:0050660", "name": "flavin adenine dinucleotide binding"}, {"accession": "GO:0016971", "name": "flavin-dependent sulfhydryl oxidase activity"}, {"accession": "GO:0016972", "name": "thiol oxidase activity"}]}, "cellular_component": {"go": [{"accession": "GO:0005789", "name": "endoplasmic reticulum membrane"}, {"accession": "GO:0000324", "name": "fungal-type vacuole"}, {"accession": "GO:0000329", "name": "fungal-type vacuole membrane"}, {"accession": "GO:0005739", "name": "mitochondrion"}]}, "biological_process": {"go": {"accession": "GO:0060904", "name": "regulation of protein folding in endoplasmic reticulum"}}}, "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 ERV2", "source_organism": "Saccharomyces cerevisiae", "uniprot": {"id": "Q12284", "start": "74", "end": "178", "coverage": "53%", "sequence": "MKQIVKRSHAIRIVAALGIIGLWMFFSSNELSIATPGLIKAKSGIDEVQGAAAEKNDARLKEIEKQTIMPLMGDDKVKKEVGRASWKYFHTLLARFPDEPTPEEREKLHTFIGLYAELYPCGECSYHFVKLIEKYPVQTSSRTAAAMWGCHIHNKVNEYLKKDIYDCATILEDYDCGCSDSDGKRVSLEKEAKQHG", "length": "196"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "4", "region_end": "25"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "31", "region_end": "49"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "51", "region_end": "65"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "71", "region_end": "90"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "99", "region_end": "104"}, {"region_type": "pfam", "region_id": "PF04777", "region_name": "Erv1 / Alr family", "region_start": "83", "region_end": "174"}]}}, {"id": "B", "name": "FAD-linked sulfhydryl oxidase ERV2", "source_organism": "Saccharomyces cerevisiae", "uniprot": {"id": "Q12284", "start": "75", "end": "179", "coverage": "53%", "sequence": "MKQIVKRSHAIRIVAALGIIGLWMFFSSNELSIATPGLIKAKSGIDEVQGAAAEKNDARLKEIEKQTIMPLMGDDKVKKEVGRASWKYFHTLLARFPDEPTPEEREKLHTFIGLYAELYPCGECSYHFVKLIEKYPVQTSSRTAAAMWGCHIHNKVNEYLKKDIYDCATILEDYDCGCSDSDGKRVSLEKEAKQHG", "length": "196"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "5", "region_end": "25"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "31", "region_end": "49"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "51", "region_end": "65"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "71", "region_end": "90"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "96", "region_end": "98"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "99", "region_end": "104"}, {"region_type": "pfam", "region_id": "PF04777", "region_name": "Erv1 / Alr family", "region_start": "83", "region_end": "174"}]}}]}, "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": "B", "support": "N/A"}]}, "related_structures": {"id": ["MF7000866", "MF7000270", "MF7000867", "MF7000868", "MF7000869", "MF7000870"]}}}