DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature (0028-0836) 2001 imex curation Lake MW., Wuebbens MM., Rajagopalan KV., Schindelin H. 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 Lake MW., Wuebbens MM., Rajagopalan KV., Schindelin H. Nature (0028-0836) 2001 IMEx amp Adenosine monophosphate 5'-Adenosine monophosphate 5'-Adenylic acid 5'-AMP 5'-O-phosphonoadenosine adenosine 5'-(dihydrogen phosphate) Adenosine 5'-monophosphate Adenosine 5'-phosphate ADENOSINE MONOPHOSPHATE adenosine phosphate Adenosine-5'-monophosphoric acid adenosine-5'P adenosini phosphas Adenylate Adenylic acid Ado5'P AMP fosfato de adenosina pA PAdo phosphate d'adenosine 5'-adenylic acid small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) moeb_ecoli Molybdopterin-synthase adenylyltransferase moeB chlN b0826 JW0810 Molybdopterin-converting factor subunit 1 adenylase MoaD protein adenylase Sulfur carrier protein MoaD adenylyltransferase protein protein ecoli Escherichia coli (strain K12) MAELSDQEMLRYNRQIILRGFDFDGQEALKDSRVLIVGLGGLGCAASQYLASAGVGNLTLLDFDTVSLSNLQRQTLHSDATVGQPKVESARDALTRINPHIAITPVNALLDDAELAALIAEHDLVLDCTDNVAVRNQLNAGCFAAKVPLVSGAAIRMEGQITVFTYQDGEPCYRCLSRLFGENALTCVEAGVMAPLIGVIGSLQAMEAIKMLAGYGKPASGKIVMYDAMTCQFREMKLMRNPGCEVCGQ DIP protein P12282 original sequence version: 134 DIP protein P12282 original sequence version: null 12C77082B3F39D7D atp ATP Adenosine 5'-triphosphate Adenosine triphosphate ADENOSINE-5'-TRIPHOSPHATE Adephos Adetol Adynol Atipi ATP Atriphos Cardenosine Fosfobion Glucobasin H4atp Myotriphos Triadenyl Triphosphaden adenosine 5'-(tetrahydrogen triphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) 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 moab-moed-1 1 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 10 direct interaction direct interaction tetrameric working 82.500%, free 79.100% 1.7A Fig. 1, Table 1 moab-moad-atp 1 4 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 3 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association tetrameric working 79.700%, free 73.200% 2.9A Fig. 2a, Table 1 moab-moad-amp 1 2 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association tetrameric working 81.200%, free 77.500% 2.1A Fig. 2b, Table 1