eF-site ID 4jit-ABCD PDB Code 4jit Chain A, B, C, D click to enlarge Title Crystal Structure of E. coli XGPRT in complex with (S)-3-(Guanin-9-yl)pyrrolidin-N-ylacetylphosphonic acid Classification TRANSFERASE Compound Xanthine phosphoribosyltransferase Source null (H0Q6L9_ECOLI) Sequence A:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGE GFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLV DDYVVDIPQDTWIEQPWDMGVVFVPPISG B:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGE GFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLV DDYVVDIPQDTWIEQPWDMGVVFVPPISGR C:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGE GFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLV DDYVVDIPQDTWIEQPWDMGVVFVPPISGR D:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISELKVLKRAEGDGEGFIVIDDL VDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIP QDTWIEQPWDMGVVFVPPISGR Description Functional site 1) chain B residue 69 type sequence R description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 2) chain B residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 3) chain B residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 4) chain B residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 5) chain B residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 6) chain B residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 7) chain B residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 8) chain B residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 9) chain B residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 10) chain B residue 140 type sequence D description BINDING SITE FOR RESIDUE 3ZF B 201 source : AC1 11) chain C residue 69 type sequence R description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 12) chain C residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 13) chain C residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 14) chain C residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 15) chain C residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 16) chain C residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 17) chain C residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 18) chain C residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 19) chain C residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 20) chain C residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 21) chain C residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZF C 201 source : AC2 22) chain A residue 88 type catalytic sequence D description 391 source MCSA : MCSA1 23) chain A residue 89 type catalytic sequence D description 391 source MCSA : MCSA1 24) chain A residue 92 type catalytic sequence D description 391 source MCSA : MCSA1 25) chain B residue 88 type catalytic sequence D description 391 source MCSA : MCSA2 26) chain B residue 89 type catalytic sequence D description 391 source MCSA : MCSA2 27) chain B residue 92 type catalytic sequence D description 391 source MCSA : MCSA2 28) chain C residue 88 type catalytic sequence D description 391 source MCSA : MCSA3 29) chain C residue 89 type catalytic sequence D description 391 source MCSA : MCSA3 30) chain C residue 92 type catalytic sequence D description 391 source MCSA : MCSA3 31) chain D residue 88 type catalytic sequence D description 391 source MCSA : MCSA4 32) chain D residue 89 type catalytic sequence D description 391 source MCSA : MCSA4 33) chain D residue 92 type catalytic sequence D description 391 source MCSA : MCSA4 34) chain A residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 40) chain D residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 46) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 47) chain C residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 48) chain D residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 51) chain C residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 52) chain D residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 55) chain B residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 56) chain B residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 57) chain C residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 58) chain C residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 59) chain D residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 60) chain D residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 61) 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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