eF-site ID 1a97-ABCD PDB Code 1a97 Chain A, B, C, D click to enlarge Title XPRTASE FROM E. COLI COMPLEXED WITH GMP Classification PHOSPHORIBOSYLTRANSFERASE Compound XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE Source Escherichia coli (strain K12) (XGPT_ECOLI) Sequence A:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVAISSYDRELKVLKRAEGDGEGFIV IDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYV VDIPQDTWIEQPWDMGVVFVPPIS B:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVAISSYDHDNQRELKVLKRAEGDGE GFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLV DDYVVDIPQDTWIEQPWDMGVVFVPPIS C:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVAISSYDHDNQRELKVLKRAEGDGE GFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLV DDYVVDIPQDTWIEQPWDMGVVFVPPIS D:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVAISSYLKVLKRAEGDGEGFIVIDD LVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDI PQDTWIEQPWDMGVVFVPPIS Description Functional site 1) chain B residue 66 type sequence D description BINDING SITE FOR RESIDUE BO3 D 301 source : AC1 2) chain B residue 67 type sequence N description BINDING SITE FOR RESIDUE BO3 D 301 source : AC1 3) chain D residue 35 type sequence V description BINDING SITE FOR RESIDUE BO3 D 301 source : AC1 4) chain D residue 37 type sequence R description BINDING SITE FOR RESIDUE BO3 D 301 source : AC1 5) chain D residue 38 type sequence G description BINDING SITE FOR RESIDUE BO3 D 301 source : AC1 6) chain D residue 88 type sequence D description BINDING SITE FOR RESIDUE BO3 D 301 source : AC1 7) chain A residue 35 type sequence V description BINDING SITE FOR RESIDUE BO3 A 302 source : AC2 8) chain A residue 36 type sequence S description BINDING SITE FOR RESIDUE BO3 A 302 source : AC2 9) chain A residue 38 type sequence G description BINDING SITE FOR RESIDUE BO3 A 302 source : AC2 10) chain A residue 88 type sequence D description BINDING SITE FOR RESIDUE BO3 A 302 source : AC2 11) chain C residue 67 type sequence N description BINDING SITE FOR RESIDUE BO3 A 302 source : AC2 12) chain C residue 35 type sequence V description BINDING SITE FOR RESIDUE BO3 C 303 source : AC3 13) chain C residue 36 type sequence S description BINDING SITE FOR RESIDUE BO3 C 303 source : AC3 14) chain C residue 38 type sequence G description BINDING SITE FOR RESIDUE BO3 C 303 source : AC3 15) chain C residue 88 type sequence D description BINDING SITE FOR RESIDUE BO3 C 303 source : AC3 16) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE BO3 B 304 source : AC4 17) chain B residue 37 type sequence R description BINDING SITE FOR RESIDUE BO3 B 304 source : AC4 18) chain B residue 38 type sequence G description BINDING SITE FOR RESIDUE BO3 B 304 source : AC4 19) chain B residue 88 type sequence D description BINDING SITE FOR RESIDUE BO3 B 304 source : AC4 20) chain B residue 69 type sequence R description BINDING SITE FOR RESIDUE 5GP B 305 source : AC5 21) chain B residue 90 type sequence L description BINDING SITE FOR RESIDUE 5GP B 305 source : AC5 22) chain B residue 92 type sequence D description BINDING SITE FOR RESIDUE 5GP B 305 source : AC5 23) chain B residue 93 type sequence T description BINDING SITE FOR RESIDUE 5GP B 305 source : AC5 24) chain B residue 94 type sequence G description BINDING SITE FOR RESIDUE 5GP B 305 source : AC5 25) chain B residue 96 type sequence T description BINDING SITE FOR RESIDUE 5GP B 305 source : AC5 26) chain B residue 134 type sequence W description BINDING SITE FOR RESIDUE 5GP B 305 source : AC5 27) chain B residue 135 type sequence I description BINDING SITE FOR RESIDUE 5GP B 305 source : AC5 28) chain C residue 69 type sequence R description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 29) chain C residue 88 type sequence D description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 30) chain C residue 90 type sequence L description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 31) chain C residue 92 type sequence D description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 32) chain C residue 93 type sequence T description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 33) chain C residue 94 type sequence G description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 34) chain C residue 95 type sequence G description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 35) chain C residue 96 type sequence T description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 36) chain C residue 115 type sequence K description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 37) chain C residue 134 type sequence W description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 38) chain C residue 135 type sequence I description BINDING SITE FOR RESIDUE 5GP C 306 source : AC6 39) chain A residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 43) chain C residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 44) chain C residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 45) chain D residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 46) chain D residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 47) chain A residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 51) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 52) chain C residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 53) chain D residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 55) chain B residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 56) chain C residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 57) chain D residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 88 type catalytic sequence D description 391 source MCSA : MCSA1 59) chain A residue 89 type catalytic sequence D description 391 source MCSA : MCSA1 60) chain A residue 92 type catalytic sequence D description 391 source MCSA : MCSA1 61) chain B residue 88 type catalytic sequence D description 391 source MCSA : MCSA2 62) chain B residue 89 type catalytic sequence D description 391 source MCSA : MCSA2 63) chain B residue 92 type catalytic sequence D description 391 source MCSA : MCSA2 64) chain C residue 88 type catalytic sequence D description 391 source MCSA : MCSA3 65) chain C residue 89 type catalytic sequence D description 391 source MCSA : MCSA3 66) chain C residue 92 type catalytic sequence D description 391 source MCSA : MCSA3 67) chain D residue 88 type catalytic sequence D description 391 source MCSA : MCSA4 68) chain D residue 89 type catalytic sequence D description 391 source MCSA : MCSA4 69) chain D residue 92 type catalytic sequence D description 391 source MCSA : MCSA4 70) chain A residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 71) chain A residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 72) chain B residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 73) chain B residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 74) chain C residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 75) chain C residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 76) chain D residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 77) chain D residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 78) 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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