eF-site ID 4jls-ABCDEHIJ PDB Code 4jls Chain A, B, C, D, E, H, I, J click to enlarge Title Crystal Structure of E. coli XGPRT in complex with (3R,4S)-4-(Guanin-9-yl)-3-hydroxypyrrolidin-1-N-ylacetylphosphonic acid Classification TRANSFERASE Compound Xanthine phosphoribosyltransferase Source Escherichia coli str. K-12 substr. MDS42 (H0Q6L9_ECOLI) Sequence A:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISGDGEGFIVIDDLVDTGGTAVA IREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPW DMGVVFVPPISGR B:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSEGDGEGFIVIDDLVDTGGTA VAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQ PWDMGVVFVPPISGR C:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISGDGEGFIVIDDLVDTGGTAVA IREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPW DMGVVFVPPISGR D:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSDGEGFIVIDDLVDTGGTAVA IREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPW DMGVVFVPPISGR E:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSGDGEGFIVIDDLVDTGGTAV AIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQP WDMGVVFVPPISGR H:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSDGEGFIVIDDLVDTGGTAVA IREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPW DMGVVFVPPISGR I:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCIDGEGFIVIDDLVDTGGTAVAIR EMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQPWDM GVVFVPPISGR J:  EKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVP GALLARELGIRHVDTVCISSYDGEGFIVIDDLVDTGGTAV AIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQDTWIEQP WDMGVVFVPPISGR Description Functional site 1) chain A residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 2) chain A residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 3) chain A residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 4) chain A residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 5) chain A residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 6) chain A residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 7) chain A residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 8) chain A residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 9) chain A residue 133 type sequence T description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 10) chain A residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 11) chain A residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZE A 201 source : AC1 12) chain B residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 13) chain B residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 14) chain B residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 15) chain B residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 16) chain B residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 17) chain B residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 18) chain B residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 19) chain B residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 20) chain B residue 133 type sequence T description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 21) chain B residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 22) chain B residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZE B 201 source : AC2 23) chain C residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 24) chain C residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 25) chain C residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 26) chain C residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 27) chain C residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 28) chain C residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 29) chain C residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 30) chain C residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 31) chain C residue 133 type sequence T description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 32) chain C residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 33) chain C residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZE C 201 source : AC3 34) chain D residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 35) chain D residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 36) chain D residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 37) chain D residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 38) chain D residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 39) chain D residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 40) chain D residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 41) chain D residue 133 type sequence T description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 42) chain D residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 43) chain D residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZE D 201 source : AC4 44) chain E residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 45) chain E residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 46) chain E residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 47) chain E residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 48) chain E residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 49) chain E residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 50) chain E residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 51) chain E residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 52) chain E residue 133 type sequence T description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 53) chain E residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 54) chain E residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZE E 201 source : AC5 55) chain H residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 56) chain H residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 57) chain H residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 58) chain H residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 59) chain H residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 60) chain H residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 61) chain H residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 62) chain H residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 63) chain H residue 133 type sequence T description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 64) chain H residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 65) chain H residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZE H 201 source : AC6 66) chain A residue 79 type sequence G description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 67) chain I residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 68) chain I residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 69) chain I residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 70) chain I residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 71) chain I residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 72) chain I residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 73) chain I residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 74) chain I residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 75) chain I residue 133 type sequence T description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 76) chain I residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 77) chain I residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZE I 201 source : AC7 78) chain J residue 90 type sequence L description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 79) chain J residue 91 type sequence V description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 80) chain J residue 92 type sequence D description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 81) chain J residue 93 type sequence T description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 82) chain J residue 94 type sequence G description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 83) chain J residue 95 type sequence G description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 84) chain J residue 96 type sequence T description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 85) chain J residue 115 type sequence K description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 86) chain J residue 133 type sequence T description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 87) chain J residue 134 type sequence W description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 88) chain J residue 135 type sequence I description BINDING SITE FOR RESIDUE 3ZE J 201 source : AC8 89) chain A residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 90) chain E residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 91) chain H residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 92) chain H residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 93) chain I residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 94) chain I residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 95) chain J residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 96) chain J residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 97) chain A residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 98) chain B residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 99) chain B residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 100) chain C residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 101) chain C residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 102) chain D residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 103) chain D residue 88 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 104) chain E residue 37 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 source Swiss-Prot : SWS_FT_FI1 105) chain E residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 106) chain H residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 107) chain I residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 108) chain J residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 109) chain A residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 110) chain B residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 111) chain C residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 112) chain D residue 134 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 source Swiss-Prot : SWS_FT_FI2 113) chain A residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 114) chain B residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 115) chain C residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 116) chain D residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 117) chain E residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 118) chain H residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 119) chain I residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 120) chain J residue 89 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9100006 source Swiss-Prot : SWS_FT_FI3 121) chain A residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 122) chain E residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 123) chain H residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 124) chain H residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 125) chain I residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 126) chain I residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 127) chain J residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 128) chain J residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 129) chain A residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 130) chain B residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 131) chain B residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 132) chain C residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 133) chain C residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 134) chain D residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 135) chain D residue 135 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 136) chain E residue 92 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 source Swiss-Prot : SWS_FT_FI4 137) chain A residue 88 type catalytic sequence D description 391 source MCSA : MCSA1 138) chain A residue 89 type catalytic sequence D description 391 source MCSA : MCSA1 139) chain A residue 92 type catalytic sequence D description 391 source MCSA : MCSA1 140) chain B residue 88 type catalytic sequence D description 391 source MCSA : MCSA2 141) chain B residue 89 type catalytic sequence D description 391 source MCSA : MCSA2 142) chain B residue 92 type catalytic sequence D description 391 source MCSA : MCSA2 143) chain C residue 88 type catalytic sequence D description 391 source MCSA : MCSA3 144) chain C residue 89 type catalytic sequence D description 391 source MCSA : MCSA3 145) chain C residue 92 type catalytic sequence D description 391 source MCSA : MCSA3 146) chain D residue 88 type catalytic sequence D description 391 source MCSA : MCSA4 147) chain D residue 89 type catalytic sequence D description 391 source MCSA : MCSA4 148) chain D residue 92 type catalytic sequence D description 391 source MCSA : MCSA4 149) chain E residue 88 type catalytic sequence D description 391 source MCSA : MCSA5 150) chain E residue 89 type catalytic sequence D description 391 source MCSA : MCSA5 151) chain E residue 92 type catalytic sequence D description 391 source MCSA : MCSA5 152) chain H residue 88 type catalytic sequence D description 391 source MCSA : MCSA6 153) chain H residue 89 type catalytic sequence D description 391 source MCSA : MCSA6 154) chain H residue 92 type catalytic sequence D description 391 source MCSA : MCSA6 155) chain I residue 88 type catalytic sequence D description 391 source MCSA : MCSA7 156) chain I residue 89 type catalytic sequence D description 391 source MCSA : MCSA7 157) chain I residue 92 type catalytic sequence D description 391 source MCSA : MCSA7 158) chain J residue 88 type catalytic sequence D description 391 source MCSA : MCSA8 159) chain J residue 89 type catalytic sequence D description 391 source MCSA : MCSA8 160) chain J residue 92 type catalytic sequence D description 391 source MCSA : MCSA8 161) 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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