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 Structural and mutational analysis of substrate recognition in kojibiose phosphorylase. Structural and mutational analysis of substrate recognition in kojibiose phosphorylase. FEBS J. (1742-464X) 2013 imex curation Okada S., Yamamoto T., Watanabe H., Nishimoto T., Chaen H., Fukuda S., Wakagi T., Fushinobu S. asfushi@mail.ecc.u-tokyo.ac.jp 13-Jan-2014: 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 asfushi@mail.ecc.u-tokyo.ac.jp Accepted 2013-NOV-18 by LUANA 2013 imex curation a4xgp2_cals8 Csac_0439 protein protein cals8 Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) MKLSEREWLIEQDKLEASGKFETCFALTNGYIGIRGINEEVFCEETPGTYIAGVFDKSTAQVTELVNLPNPIGLRIYINREFLNPLKCEILEFKRVLDLKQGILYRKLRLKDVKGRITTIEGFRFVSMNNKNLIVQKYDVVCENYSAVLNVESFIDATTVNSKDVPNDRVKHYEIDKKKDFADGIYLGITTKDKKYKVGIASSTKVLLNNQRCYFNRFTKDLGYIITENFEVEAKQGERYEIEKLTVLVSSREKNVGDVFETCTNKLKEFETKSAEKLLFEHIEEYKRLWDVANIDIVGDEVANKSVKFNIFHLISMANPEDEHVSLGAKGLHGEGYKGHVFWDTEIFMLPFYIYTNPAAAKAMLMYRYNLLDAARENARKNGYKGAQFPWESADTGEEETPKWGYDYLGNPVRIWTGDIEYHISADIAYAVMNYVRATDDIDFLLNYGSEIIIETARFWASICKYNKEKGRYEINDVIGPDEFHEHCNNNAYTNYLAKWNLLKASELCNLLLEKYPKYFEKLSKKINLSDEEPFVWQEIASKIYIPYHPDKKLIEQFEGYFNLKDFVIKEYDQNNMPVWPEGVELDKLNNYQLIKQADVVMLLYLLGEEFDDQTKKINYDYYEKRTMHKSSLSPSIYALMGVRVGETNRAYINFMRTALTDLEDNQGNTHLGIHAASLGGTWQALVFGFGGISIEKDDVLSVNPWLPEKWESLKFSIWWKGNLLDFKITKDNVEVKKRVEKGNVKLKIKGQEAII 9666D2B21B66B228 a4xgp2 1 CsKP 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f1c t1 The crystal structure of CsKP was solved by molecular replacement using the LbMP structure (1H54) as the search model. The complex structure with glucose and Pi (Glc-PO4) was determined at 2.05 Å resolution (Table 1). The Glc-PO4 crystal belongs to the space group P1 and contains four CsKP molecules per asymmetric unit. The atoms in all four chains are almost identical, as the root mean square deviations (RMSDs) for Cα atoms between all pairs are within 0.24 Å. We therefore describe chain A unless otherwise noted. The complex structure with kojibiose and sulfate ion (kojibiose-SO4) was determined at 2.80 Å resolution. The kojibiose-SO4 crystal belongs to the space group I422 and contains one CsKP molecule in the asymmetric unit. The main chain trace of the kojibiose-SO4 structure is almost identical to the Glc-PO4 structure, as RMSDs for Cα atoms to the all four chains are less than 0.36 Å.