MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3. The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3. FEBS J. (1742-464X) 2012 imex curation Joyce MG., Ekanem IS., Roitel O., Dunford AJ., Neeli R., Girvan HM., Baker GJ., Curtis RA., Munro AW., Leys D. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Joyce MG., Ekanem IS., Roitel O., Dunford AJ., Neeli R., Girvan HM., Baker GJ., Curtis RA., Munro AW., Leys D. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3. The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3. FEBS J. (1742-464X) 2012 imex curation Joyce MG., Ekanem IS., Roitel O., Dunford AJ., Neeli R., Girvan HM., Baker GJ., Curtis RA., Munro AW., Leys D. 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 Joyce MG., Ekanem IS., Roitel O., Dunford AJ., Neeli R., Girvan HM., Baker GJ., Curtis RA., Munro AW., Leys D. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation cpxb_bacmb Bifunctional cytochrome P450/NADPH--P450 reductase cyp102A1 Cytochrome P450(BM-3) cyp102 Cytochrome P450BM-3 Fatty acid monooxygenase Flavocytochrome P450 BM3 BG04_163 protein protein bacmb bacmb MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGIPSPSTEQSAKKVRKKAENAHNTPLLVLYGSNMGTAEGTARDLADIAMSKGFAPQVATLDSHAGNLPREGAVLIVTASYNGHPPDNAKQFVDWLDQASADEVKGVRYSVFGCGDKNWATTYQKVPAFIDETLAAKGAENIADRGEADASDDFEGTYEEWREHMWSDVAAYFNLDIENSEDNKSTLSLQFVDSAADMPLAKMHGAFSTNVVASKELQQPGSARSTRHLEIELPKEASYQEGDHLGVIPRNYEGIVNRVTARFGLDASQQIRLEAEEEKLAHLPLAKTVSVEELLQYVELQDPVTRTQLRAMAAKTVCPPHKVELEALLEKQAYKEQVLAKRLTMLELLEKYPACEMKFSEFIALLPSIRPRYYSISSSPRVDEKQASITVSVVSGEAWSGYGEYKGIASNYLAELQEGDTITCFISTPQSEFTLPKDPETPLIMVGPGTGVAPFRGFVQARKQLKEQGQSLGEAHLYFGCRSPHEDYLYQEELENAQSEGIITLHTAFSRMPNQPKTYVQHVMEQDGKKLIELLDQGAHFYICGDGSQMAPAVEATLMKSYADVHQVSEADARLWLQQLEEKGRYAKDVWAG mint B0BE61F8A2EE33D5 cyp102a1 1 P450 BM-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P14779:p.Cys1000Ala mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain C A Tue Jul 12 10:14:40 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 18:03:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys1000ala' Tue Jun 30 16:34:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys1000Ala' P14779:p.Cys774Ala mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain C A Tue Jul 12 10:11:35 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 18:24:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys774ala' Tue Jun 30 17:22:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys774Ala' binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.0 direct interaction direct interaction f1 mint Our studies of the WT FAD domain using MALLS were consistent with the findings of Black and Martin, indicating that both monomer, dimer and some higher molecular mass aggregates were present (with monomer:dimer in an ~60%:40% ratio). When the peak fractions for the dimeric form were separated, pooled and reloaded on this system, a single dimeric species was obtained with apparent average molecular mass 86.4 ± 3.8 kDa, close to that predicted for the FAD domain dimer (88.4 kDa in absence of the initiator methionine). However, analysis of the same dimer peak fraction sample pre-treated with the reductant dithiothreitol (DTT) and then with iodoacetamide (in order to covalently modify any exposed cysteine residues) provided a different result, with both monomer (44.0 ± 2.1 kDa, ~25%) and dimer (86.3 ± 5.6 kDa, ~75%) present (Figure 1). cyp102a1-1 2 P450 BM-3 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 2.0 direct interaction direct interaction f2 t1 mint The final refined model of the ligand-free BM3 FAD domain C773A/C999A mutant contains two molecules per asymmetric unit, and the structure was resolved to 2.4 Å.