eF-site ID 1c7z-A PDB Code 1c7z Chain A click to enlarge Title REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE Classification HYDROLASE Compound FRUCTOSE-2,6-BISPHOSPHATASE Source null (F261_RAT) Sequence A:  MRSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANF IRSQGISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEID AGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYED LVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSD ELPYLKCPLHTVLKLTPVAYGCRVESIYLNV Description Functional site 1) chain A residue 8 type sequence R description BINDING SITE FOR RESIDUE PO4 A 401 source : AC1 2) chain A residue 9 type sequence H description BINDING SITE FOR RESIDUE PO4 A 401 source : AC1 3) chain A residue 15 type sequence N description BINDING SITE FOR RESIDUE PO4 A 401 source : AC1 4) chain A residue 58 type sequence R description BINDING SITE FOR RESIDUE PO4 A 401 source : AC1 5) chain A residue 78 type sequence E description BINDING SITE FOR RESIDUE PO4 A 401 source : AC1 6) chain A residue 143 type sequence H description BINDING SITE FOR RESIDUE PO4 A 401 source : AC1 7) chain A residue 144 type sequence Q description BINDING SITE FOR RESIDUE PO4 A 401 source : AC1 8) chain A residue 89 type sequence Y description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 9) chain A residue 103 type sequence R description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 10) chain A residue 107 type sequence K description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 11) chain A residue 118 type sequence Y description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 12) chain A residue 144 type sequence Q description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 13) chain A residue 145 type sequence A description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 14) chain A residue 148 type sequence R description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 15) chain A residue 10 type ACT_SITE sequence G description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 79 type ACT_SITE sequence I description Proton donor/acceptor => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 9 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 59 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 181 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 16 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 6-15 type prosite sequence LCRHGESELN description PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN source prosite : PS00175 22) chain A residue 22 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 149 type BINDING sequence C description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 90 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 104 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 108 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 119 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 145 type BINDING sequence A description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 101 type BINDING sequence A description BINDING => ECO:0000269|Ref.15 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 144 type SITE sequence Q description Transition state stabilizer => ECO:0000250|UniProtKB:P00950 source Swiss-Prot : SWS_FT_FI6

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