IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat. Struct. Biol. (1072-8368) 2001 imex curation Rudolph M.J., Wuebbens M.M., Rajagopalan K.V., Schindelin H. hermann.schindelin@sunysb.edu 02-Aug-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column ms participant Identification by mass spectrometry ms participant Rudolph M.J., Wuebbens M.M., Rajagopalan K.V., Schindelin H. hermann.schindelin@sunysb.edu Accepted 2013-JUL-15 by MGT 02-Aug-2013: Contacted by IntAct-Help. Nat. Struct. Biol. (1072-8368) 2001 Only protein-protein interactions imex curation Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat. Struct. Biol. (1072-8368) 2001 imex curation Rudolph M.J., Wuebbens M.M., Rajagopalan K.V., Schindelin H. hermann.schindelin@sunysb.edu 02-Aug-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Rudolph M.J., Wuebbens M.M., Rajagopalan K.V., Schindelin H. hermann.schindelin@sunysb.edu Accepted 2013-JUL-15 by MGT 02-Aug-2013: Contacted by IntAct-Help. Nat. Struct. Biol. (1072-8368) 2001 Only protein-protein interactions imex curation moad_ecoli Molybdopterin synthase sulfur carrier subunit Molybdenum cofactor biosynthesis protein D Molybdopterin-converting factor small subunit moaD chlA4 chlM b0784 JW0767 MPT synthase subunit 1 Molybdopterin-converting factor subunit 1 Sulfur carrier protein MoaD protein protein ecoli Escherichia coli (strain K12) MIKVLFFAQVRELVGTDATEVAADFPTVEALRQHMAAQSDRWALALEDGKLLAAVNQTLVSFDHPLTDGDEVAFFPPVTGG DIP protein P30748 original sequence version: 147 DIP protein P30748 original sequence version: null 1E0A440520EE82F4 moae_ecoli Molybdopterin synthase catalytic subunit Molybdopterin-converting factor subunit 2 Molybdenum cofactor biosynthesis protein E Molybdopterin-converting factor large subunit moaE chlA5 b0785 JW0768 MPT synthase subunit 2 protein protein ecoli Escherichia coli (strain K12) MAETKIVVGPQPFSVGEEYPWLAERDEDGAVVTFTGKVRNHNLGDSVNALTLEHYPGMTEKALAEIVDEARNRWPLGRVTVIHRIGELWPGDEIVFVGVTSAHRSSAFEAGQFIMDYLKTRAPFWKREATPEGDRWVEARESDQQAAKRW DIP protein P30749 original sequence version: null 6E40776E5A6E85BB moad-moae-2 1 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component P30748:p.Ile2Val mutation mutation certain certain sequence position certain certain certain sequence position certain I V Wed May 02 17:25:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile2val' Tue Jun 30 19:00:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile2Val' ecoli Escherichia coli (strain K12) physical association physical association Fig. 2a Addition of MoeB (P12282) thiocarboxylates the MoaD-Gly81 (Fig. 2b). Long-term storage of the complex at 4C results in a stable, covalently linked complex of MoaD-MoaE without loss of the sulphur as H2S (Fig. 2c). moad-moae-3 2 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component P30748:p.Ile2Val mutation mutation certain certain sequence position certain certain certain sequence position certain I V Wed May 02 15:33:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile2val' Tue Jun 30 17:13:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile2Val' ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 3 A second crystal with slightly less resolution can be found under wwwpdb = 1fma. 1.45 A R = 0.15; Rwork = 0.15; Rfree = 0.18