eF-site ID 1dku-A PDB Code 1dku Chain A click to enlarge Title CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION. Classification TRANSFERASE Compound PROTEIN (PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE) Source Bacillus subtilis (strain 168) (KPRS_BACSU) Sequence A:  NLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQI NIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASA KTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGAT RVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLED IVIVSPDHGGVTRARKLADRLKAPIAIIDKRMNIVGNIEG KTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVL SGPAVERINNSTIKELVVTNSIKLKIERFKQLSVGPLLAE AIIRVHEQQSVSYLF Description Functional site 1) chain A residue 105 type sequence K description BINDING SITE FOR RESIDUE AP2 B 1001 source : AC1 2) chain A residue 108 type sequence S description BINDING SITE FOR RESIDUE AP2 B 1001 source : AC1 3) chain A residue 109 type sequence R description BINDING SITE FOR RESIDUE AP2 B 1001 source : AC1 4) chain A residue 52 type sequence S description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 5) chain A residue 54 type sequence R description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 6) chain A residue 140 type sequence Q description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 7) chain A residue 148 type sequence D description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 8) chain A residue 149 type sequence H description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 9) chain A residue 310 type sequence S description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 10) chain A residue 311 type sequence V description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 11) chain A residue 312 type sequence S description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 12) chain A residue 315 type sequence F description BINDING SITE FOR RESIDUE AP2 A 1002 source : AC2 13) chain A residue 101 type sequence R description BINDING SITE FOR RESIDUE ABM A 1003 source : AC3 14) chain A residue 102 type sequence Q description BINDING SITE FOR RESIDUE ABM A 1003 source : AC3 15) chain A residue 106 type sequence A description BINDING SITE FOR RESIDUE ABM A 1003 source : AC3 16) chain A residue 135 type sequence H description BINDING SITE FOR RESIDUE ABM A 1003 source : AC3 17) chain A residue 40 type sequence F description BINDING SITE FOR RESIDUE ABM B 1004 source : AC4 18) chain A residue 42 type sequence D description BINDING SITE FOR RESIDUE ABM B 1004 source : AC4 19) chain A residue 44 type sequence E description BINDING SITE FOR RESIDUE ABM B 1004 source : AC4 20) chain A residue 197 type ACT_SITE sequence K description ACT_SITE => ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:16008562 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 223 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-Rule:MF_00583 source Swiss-Prot : SWS_FT_FI6 22) chain A residue 219-231 type prosite sequence AILIDDIIDTAGT description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. AILIDDIIDTAgT source prosite : PS00103 23) chain A residue 133-148 type prosite sequence DLHAPQIQGFFDIPID description PRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHApQIQGFFdiPID source prosite : PS00114 24) chain A residue 227 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10742175, ECO:0000269|PubMed:11790837, ECO:0007744|PDB:1DKR, ECO:0007744|PDB:1IBS source Swiss-Prot : SWS_FT_FI7 25) chain A residue 42 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:10742175 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 101 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:11790837, ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU, ECO:0007744|PDB:1IBS source Swiss-Prot : SWS_FT_FI3 27) chain A residue 105 type BINDING sequence K description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU source Swiss-Prot : SWS_FT_FI4 28) chain A residue 109 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU source Swiss-Prot : SWS_FT_FI4 29) chain A residue 140 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU source Swiss-Prot : SWS_FT_FI4 30) chain A residue 148 type BINDING sequence D description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU source Swiss-Prot : SWS_FT_FI4 31) chain A residue 310 type BINDING sequence S description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU source Swiss-Prot : SWS_FT_FI4 32) chain A residue 135 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837, ECO:0007744|PDB:1IBS source Swiss-Prot : SWS_FT_FI5 33) chain A residue 174 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837, ECO:0007744|PDB:1IBS source Swiss-Prot : SWS_FT_FI5

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