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 [3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis. [3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis. Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 1998 Rousset M., Montet Y., Guigliarelli B., Forget N., Asso M., Bertrand P., Fontecilla-Camps JC., Hatchikian EC. no in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Rousset M., Montet Y., Guigliarelli B., Forget N., Asso M., Bertrand P., Fontecilla-Camps JC., Hatchikian EC. no Proc. Natl. Acad. Sci. U.S.A. (0027-8424) 1998 phnl_desfr Periplasmic [NiFe] hydrogenase large subunit hydB NiFe hydrogenlyase large chain protein protein desfr Desulfovibrio fructosivorans MAESKPTPQSTFTGPIVVDPITRIEGHLRIMVEVENGKVKDAWSSSQLFRGLEIILKGRDPRDAQHFTQRACGVCTYVHALASSRCVDDAVKVSIPANARMMRNLVMASQYLHDHLVHFYHLHALDWVDVTAALKADPNKAAKLAASIAPARPGNSAKALKAVQDKLKAFVESGQLGIFTNAYFLGGHKAYYLPPEVDLIATAHYLEALHMQVKAASAMAILGGKNPHTQFTVVGGCSNYQGLTKDPLANYLALSKEVCQFVNECYIPDLLAVAGFYKDWGGIGGTSNYLAFGEFATDDSSPEKHLATSQFPSGVITGRDLGKVDNVDLGAIYEDVKYSWYAPGGDGKHPYDGVTDPKYTKLDDKDHYSWMKAPRYKGKAMEVGPLARTFIAYAKGQPDFKKVVDMVLGKLSVPATALHSTLGRTAARGIETAIVCANMEKWIKEMADSGAKDNTLCAKWEMPEESKGVGLADAPRGALSHWIRIKGKKIDNFQLVVPSTWNLGPRGAQGDKSPVEEALIGTPIADPKRPVEILRTVHAFDPCIACGVHVIEPETNEILKFKVC mint AB3EBF47F364D849 phns_desfr Periplasmic [NiFe] hydrogenase small subunit hydA NiFe hydrogenlyase small chain protein protein desfr Desulfovibrio fructosivorans MNFSVGLGRDDAEKRLVQNGVSRRDFMKFCATVAAAMGMGPAFAPKVAEALTAKHRPSVVWLHNAECTGCTEAAIRTIKPYIDALILDTISLDYQETIMAAAGEAAEAALHQALEGKDGYYLVVEGGLPTIDGGQWGMVAGHPMIETTKKAAAKAKGIICIGTCSAYGGVQKAKPNPSQAKGVSEALGVKTINIPGCPPNPINFVGAVVHVLTKGIPDLDENGRPKLFYGELVHDNCPRLPHFEASEFAPSFDSEEAKKGFCLYELGCKGPVTYNNCPKVLFNQVNWPVQAGHPCLGCSEPDFWDTMTPFYEQG mint 48BE00FE51D23A68 hyda-hydb-1 1 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1frf, P18188 is chain L and P18187 is chain S Resolution 2.700 mint