eF-site ID 1a3c-A PDB Code 1a3c Chain A click to enlarge Title PYRR, THE BACILLUS SUBTILIS PYRIMIDINE BIOSYNTHETIC OPERON REPRESSOR, DIMERIC FORM Classification TRANSCRIPTION REGULATION Compound PYRIMIDINE OPERON REGULATORY PROTEIN PYRR Source Bacillus subtilis (strain 168) (PYRR_BACSU) Sequence A:  QKAVILDEQAIRRALTRIAHEMIERNKCILVGIKTRGIYL AKRLAERIEQIEGNPVTVGEIDITLYRNDEPLVKGADIPV DITDQKVILVDDVLYTGRTVRAGMDALVDVGRPSSIQLAV LVDRGHRELPIRADYIGKNIPTSKSEKVMVQLDEVDQNDL VAIYEN Description Functional site 1) chain A residue 105 type sequence D description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 2) chain A residue 106 type sequence D description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 3) chain A residue 107 type sequence V description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 4) chain A residue 108 type sequence L description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 5) chain A residue 109 type sequence Y description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 6) chain A residue 110 type sequence T description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 7) chain A residue 111 type sequence G description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 8) chain A residue 112 type sequence R description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 9) chain A residue 113 type sequence T description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 10) chain A residue 40 type sequence K description DUAL SITE: BINDING SITE FOR SUBSTRATE PRPP IN THIS AND OTHER MEMBERS OF THE TYPE I PHOSPHORIBOSYLTRANSFERASE (PRTASE) FAMILY OF ENZYMES, AND SULFATE ION BINDING SITE. source : PRA 11) chain A residue 10 type sequence E description SM3+ ION BINDING SITE. THE SM3+ ION LIES ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS, AND ISOCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS AND THEIR SYMMETRY RELATED ATOMS. source : SM1 12) chain A residue 167 type sequence D description SM3+ ION BINDING SITE. THE SM3+ ION LIES ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS, AND ISOCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS AND THEIR SYMMETRY RELATED ATOMS. source : SM1 13) chain A residue 173 type sequence D description SM3+ ION BINDING SITE. THE SM3+ ION LIES ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS, AND ISOCTAHEDRALLY COORDINATED BY THE OXYGENS OF THREE AMINO ACID SIDE CHAINS AND THEIR SYMMETRY RELATED ATOMS. source : SM1 14) chain A residue 10 type sequence E description BINDING SITE FOR RESIDUE SM A 182 source : AC1 15) chain A residue 10 type sequence E description BINDING SITE FOR RESIDUE SM A 182 source : AC1 16) chain A residue 167 type sequence D description BINDING SITE FOR RESIDUE SM A 182 source : AC1 17) chain A residue 167 type sequence D description BINDING SITE FOR RESIDUE SM A 182 source : AC1 18) chain A residue 173 type sequence D description BINDING SITE FOR RESIDUE SM A 182 source : AC1 19) chain A residue 173 type sequence D description BINDING SITE FOR RESIDUE SM A 182 source : AC1 20) chain A residue 40 type sequence K description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 21) chain A residue 105 type sequence D description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 22) chain A residue 107 type sequence V description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 23) chain A residue 108 type sequence L description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 24) chain A residue 109 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 25) chain A residue 110 type sequence T description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 26) chain A residue 111 type sequence G description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 27) chain A residue 112 type sequence R description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 28) chain A residue 113 type sequence T description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 29) chain A residue 114 type sequence V description BINDING SITE FOR RESIDUE SO4 A 184 source : AC3 30) chain A residue 41 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 105 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 138 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 162 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1

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