eF-site ID 1c7z-AB PDB Code 1c7z Chain A, B 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 B:  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 B residue 8 type sequence R description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 9) chain B residue 9 type sequence H description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 10) chain B residue 15 type sequence N description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 11) chain B residue 58 type sequence R description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 12) chain B residue 78 type sequence E description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 13) chain B residue 143 type sequence H description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 14) chain B residue 144 type sequence Q description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 15) chain A residue 89 type sequence Y description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 16) chain A residue 103 type sequence R description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 17) chain A residue 107 type sequence K description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 18) chain A residue 118 type sequence Y description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 19) chain A residue 144 type sequence Q description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 20) chain A residue 145 type sequence A description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 21) chain A residue 148 type sequence R description BINDING SITE FOR RESIDUE G3H A 501 source : AC3 22) chain B residue 78 type sequence E description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 23) chain B residue 89 type sequence Y description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 24) chain B residue 103 type sequence R description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 25) chain B residue 107 type sequence K description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 26) chain B residue 118 type sequence Y description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 27) chain B residue 144 type sequence Q description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 28) chain B residue 145 type sequence A description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 29) chain B residue 148 type sequence R description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 30) chain A residue 10 type ACT_SITE sequence G description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 10 type ACT_SITE sequence G description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 79 type ACT_SITE sequence I description Proton donor/acceptor => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 79 type ACT_SITE sequence I description Proton donor/acceptor => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 9 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 59 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 181 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 9 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 16 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 39) chain B residue 59 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 40) chain B residue 181 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 16 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 6-15 type prosite sequence LCRHGESELN description PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN source prosite : PS00175 43) chain A residue 22 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 44) chain B residue 104 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 45) chain B residue 108 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 46) chain B residue 119 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 47) chain B residue 145 type BINDING sequence A description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 48) chain B residue 149 type BINDING sequence C description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 49) chain A residue 149 type BINDING sequence C description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 50) chain B residue 22 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 51) chain B residue 90 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 52) chain A residue 90 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 104 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 108 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 119 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 145 type BINDING sequence A description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 57) chain A residue 101 type BINDING sequence A description BINDING => ECO:0000269|Ref.15 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 101 type BINDING sequence A description BINDING => ECO:0000269|Ref.15 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 144 type SITE sequence Q description Transition state stabilizer => ECO:0000250|UniProtKB:P00950 source Swiss-Prot : SWS_FT_FI6 60) chain B residue 144 type SITE sequence Q description Transition state stabilizer => ECO:0000250|UniProtKB:P00950 source Swiss-Prot : SWS_FT_FI6

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