eF-site ID 1a96-ABCD PDB Code 1a96 Chain A, B, C, D click to enlarge Title XPRTASE FROM E. COLI WITH BOUND CPRPP AND XANTHINE Classification PHOSPHORIBOSYLTRANSFERASE Compound XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE Source Escherichia coli (strain K12) (XGPT_ECOLI) Sequence A:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSYNQRELKVLKRAEGDGEGFI VIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDY VVDIPQDTWIEQPWDMGVVFVPPIS B:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGE GFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLV DDYVVDIPQDTWIEQPWDMGVVFVPPISGR C:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGE GFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLV DDYVVDIPQDTWIEQPWDMGVVFVPPISGR D:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSYRELKVLKRAEGDGEGFIVI DDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVV DIPQDTWIEQPWDMGVVFVPPISGR Description Functional site 1) chain A residue 53 type sequence R description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 2) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 3) chain B residue 37 type sequence R description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 4) chain B residue 38 type sequence G description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 5) chain B residue 69 type sequence R description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 6) chain B residue 88 type sequence D description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 7) chain B residue 89 type sequence D description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 8) chain B residue 90 type sequence L description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 9) chain B residue 92 type sequence D description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 10) chain B residue 93 type sequence T description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 11) chain B residue 94 type sequence G description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 12) chain B residue 95 type sequence G description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 13) chain B residue 96 type sequence T description BINDING SITE FOR RESIDUE PCP B 301 source : AC3 14) chain C residue 37 type sequence R description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 15) chain C residue 38 type sequence G description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 16) chain C residue 69 type sequence R description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 17) chain C residue 88 type sequence D description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 18) chain C residue 89 type sequence D description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 19) chain C residue 90 type sequence L description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 20) chain C residue 92 type sequence D description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 21) chain C residue 93 type sequence T description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 22) chain C residue 94 type sequence G description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 23) chain C residue 95 type sequence G description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 24) chain C residue 96 type sequence T description BINDING SITE FOR RESIDUE PCP C 302 source : AC4 25) chain C residue 92 type sequence D description BINDING SITE FOR RESIDUE XAN C 303 source : AC5 26) chain C residue 115 type sequence K description BINDING SITE FOR RESIDUE XAN C 303 source : AC5 27) chain C residue 134 type sequence W description BINDING SITE FOR RESIDUE XAN C 303 source : AC5 28) chain C residue 135 type sequence I description BINDING SITE FOR RESIDUE XAN C 303 source : AC5 29) chain B residue 92 type sequence D description BINDING SITE FOR RESIDUE XAN B 304 source : AC6 30) chain B residue 115 type sequence K description BINDING SITE FOR RESIDUE XAN B 304 source : AC6 31) chain B residue 134 type sequence W description BINDING SITE FOR RESIDUE XAN B 304 source : AC6 32) chain B residue 135 type sequence I description BINDING SITE FOR RESIDUE XAN B 304 source : AC6 33) chain B residue 67 type sequence N description BINDING SITE FOR RESIDUE BO3 D 305 source : AC7 34) chain D residue 35 type sequence V description BINDING SITE FOR RESIDUE BO3 D 305 source : AC7 35) chain D residue 36 type sequence S description BINDING SITE FOR RESIDUE BO3 D 305 source : AC7 36) chain D residue 37 type sequence R description BINDING SITE FOR RESIDUE BO3 D 305 source : AC7 37) chain D residue 38 type sequence G description BINDING SITE FOR RESIDUE BO3 D 305 source : AC7 38) chain D residue 88 type sequence D description BINDING SITE FOR RESIDUE BO3 D 305 source : AC7 39) chain A residue 35 type sequence V description BINDING SITE FOR RESIDUE BO3 A 306 source : AC8 40) chain A residue 36 type sequence S description BINDING SITE FOR RESIDUE BO3 A 306 source : AC8 41) chain A residue 38 type sequence G description BINDING SITE FOR RESIDUE BO3 A 306 source : AC8 42) chain A residue 88 type sequence D description BINDING SITE FOR RESIDUE BO3 A 306 source : AC8 43) chain C residue 67 type sequence N description BINDING SITE FOR RESIDUE BO3 A 306 source : AC8 44) chain A residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 48) chain C residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 49) chain C residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 50) chain D residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 51) chain D residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 54) chain B residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 55) chain B residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 56) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 57) chain C residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 58) chain D residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 59) chain D residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 61) chain B residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 62) chain C residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 63) chain D residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 64) chain A residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 65) chain A residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 66) chain B residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 67) chain B residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 68) chain C residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 69) chain C residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 70) chain D residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 71) chain D residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 72) chain A residue 88 type catalytic sequence D description 391 source MCSA : MCSA1 73) chain A residue 89 type catalytic sequence D description 391 source MCSA : MCSA1 74) chain A residue 92 type catalytic sequence D description 391 source MCSA : MCSA1 75) chain B residue 88 type catalytic sequence D description 391 source MCSA : MCSA2 76) chain B residue 89 type catalytic sequence D description 391 source MCSA : MCSA2 77) chain B residue 92 type catalytic sequence D description 391 source MCSA : MCSA2 78) chain C residue 88 type catalytic sequence D description 391 source MCSA : MCSA3 79) chain C residue 89 type catalytic sequence D description 391 source MCSA : MCSA3 80) chain C residue 92 type catalytic sequence D description 391 source MCSA : MCSA3 81) chain D residue 88 type catalytic sequence D description 391 source MCSA : MCSA4 82) chain D residue 89 type catalytic sequence D description 391 source MCSA : MCSA4 83) chain D residue 92 type catalytic sequence D description 391 source MCSA : MCSA4 84) chain A residue 84-96 type prosite sequence FIVIDDLVDTGGT description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. FIVIDDLVDTGgT source prosite : PS00103

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