eF-site ID 1nul-AB PDB Code 1nul Chain A, B click to enlarge Title XPRTASE FROM E. COLI Classification PHOSPHORIBOSYLTRANSFERASE Compound XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence A:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSLKVLKRAEGDGEGFIVIDDL VDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIP QDTWIEQPWDMGVVFVPPISGR B:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCIVLKRAEGDGEGFIVIDDLVDTT AVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIE QPWDMGVVFVPPISGR Description Functional site 1) chain A residue 53 type sequence R description BINDING SITE FOR RESIDUE SO4 B 301 source : AC1 2) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE SO4 B 301 source : AC1 3) chain B residue 37 type sequence R description BINDING SITE FOR RESIDUE SO4 B 301 source : AC1 4) chain B residue 38 type sequence G description BINDING SITE FOR RESIDUE SO4 B 301 source : AC1 5) chain B residue 106 type sequence K description BINDING SITE FOR RESIDUE SO4 B 301 source : AC1 6) chain A residue 37 type sequence R description BINDING SITE FOR RESIDUE SO4 A 302 source : AC2 7) chain A residue 38 type sequence G description BINDING SITE FOR RESIDUE SO4 A 302 source : AC2 8) chain B residue 89 type sequence D description BINDING SITE FOR RESIDUE MG B 501 source : AC3 9) chain A residue 88 type sequence D description BINDING SITE FOR RESIDUE MG A 502 source : AC4 10) chain A residue 89 type sequence D description BINDING SITE FOR RESIDUE MG A 502 source : AC4 11) chain A residue 88 type catalytic sequence D description 391 source MCSA : MCSA1 12) chain A residue 89 type catalytic sequence D description 391 source MCSA : MCSA1 13) chain A residue 92 type catalytic sequence D description 391 source MCSA : MCSA1 14) chain B residue 88 type catalytic sequence D description 391 source MCSA : MCSA2 15) chain B residue 89 type catalytic sequence D description 391 source MCSA : MCSA2 16) chain B residue 92 type catalytic sequence D description 391 source MCSA : MCSA2 17) chain A residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 26) chain B residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 84-96 type prosite sequence FIVIDDLVDTGGT description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. FIVIDDLVDTGgT source prosite : PS00103 28) chain A residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 29) chain B residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3

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