eF-site ID 1c7z-B PDB Code 1c7z Chain B click to enlarge Title REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE Classification HYDROLASE Compound FRUCTOSE-2,6-BISPHOSPHATASE Source Rattus norvegicus (Rat) (F261_RAT) Sequence B:  MRSIYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANF IRSQGISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEID AGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYED LVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSD ELPYLKCPLHTVLKLTPVAYGCRVESIYLNV Description Functional site 1) chain B residue 8 type sequence R description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 2) chain B residue 9 type sequence H description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 3) chain B residue 15 type sequence N description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 4) chain B residue 58 type sequence R description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 5) chain B residue 78 type sequence E description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 6) chain B residue 143 type sequence H description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 7) chain B residue 144 type sequence Q description BINDING SITE FOR RESIDUE PO4 B 402 source : AC2 8) chain B residue 78 type sequence E description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 9) chain B residue 89 type sequence Y description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 10) chain B residue 103 type sequence R description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 11) chain B residue 107 type sequence K description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 12) chain B residue 118 type sequence Y description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 13) chain B residue 144 type sequence Q description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 14) chain B residue 145 type sequence A description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 15) chain B residue 148 type sequence R description BINDING SITE FOR RESIDUE G3H B 502 source : AC4 16) chain B residue 10 type ACT_SITE sequence G description Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 79 type ACT_SITE sequence I description Proton donor/acceptor => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 9 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 19) chain B residue 16 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 59 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 181 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q16875 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 104 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 108 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 119 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 145 type BINDING sequence A description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 26) chain B residue 149 type BINDING sequence C description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 27) chain B residue 22 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 90 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9253407 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 101 type BINDING sequence A description BINDING => ECO:0000269|Ref.15 source Swiss-Prot : SWS_FT_FI5 30) 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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