eF-site ID 1a98-AB PDB Code 1a98 Chain A, B 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 GALLARELGIRHVDTVAIGDGEGFIVIDDLVDTAVAIREM YPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPWDMGV VFVPPISGR B:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVAISGEGFIVIDDLVDTTAVAIREM YPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPWDMGV VFVPPIS Description Functional site 1) chain A residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 2) chain A residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 4) chain B residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 7) chain A residue 88 type catalytic sequence D description 391 source MCSA : MCSA1 8) chain A residue 89 type catalytic sequence D description 391 source MCSA : MCSA1 9) chain A residue 92 type catalytic sequence D description 391 source MCSA : MCSA1 10) chain B residue 88 type catalytic sequence D description 391 source MCSA : MCSA2 11) chain B residue 89 type catalytic sequence D description 391 source MCSA : MCSA2 12) chain B residue 92 type catalytic sequence D description 391 source MCSA : MCSA2 13) chain A residue 84-96 type prosite sequence FIVIDDLVDT description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. FIVIDDLVDTGgT source prosite : PS00103 14) chain A residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 18) chain B residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 19) chain B residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4

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