eF-site ID 5pzt-ABCDEFGH PDB Code 5pzt Chain A, B, C, D, E, F, G, H click to enlarge Title Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-(3-ethyl-4-phenylphenyl)sulfonylurea Classification HYDROLASE/HYDROLASE INHIBITOR Compound Fructose-1,6-bisphosphatase 1 Source (Q2TU34_HUMAN) Sequence A:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAI IVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKS TDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNC FMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAV TEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFL YPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVL DVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS B:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIV EPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTD EPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFM LDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAVTE YIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYP ANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDV IPTDIHQRAPVILGSPDDVLEFLKVYEKHS C:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIV EPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTD EPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFM LDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAVTE YIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYP ANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDV IPTDIHQRAPVILGSPDDVLEFLKVYEKHS D:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIV EPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTD EPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFM LDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAVTE YIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYP ANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDV IPTDIHQRAPVILGSPDDVLEFLKVYEKHS E:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAI IVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKS TDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNC FMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAV TEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFL YPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVL DVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS F:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIV EPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTD EPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFM LDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAVTE YIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYP ANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDV IPTDIHQRAPVILGSPDDVLEFLKVYEKHS G:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIV EPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTD EPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFM LDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAVTE YIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYP ANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDV IPTDIHQRAPVILGSPDDVLEFLKVYEKHS H:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIV EPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTD EPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFM LDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAVTE YIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYP ANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDV IPTDIHQRAPVILGSPDDVLEFLKVYEKHS Description Functional site 1) chain A residue 20 type sequence E description binding site for residue 947 A 401 source : AC1 2) chain A residue 21 type sequence G description binding site for residue 947 A 401 source : AC1 3) chain A residue 22 type sequence R description binding site for residue 947 A 401 source : AC1 4) chain A residue 26 type sequence G description binding site for residue 947 A 401 source : AC1 5) chain A residue 27 type sequence T description binding site for residue 947 A 401 source : AC1 6) chain A residue 28 type sequence G description binding site for residue 947 A 401 source : AC1 7) chain A residue 30 type sequence L description binding site for residue 947 A 401 source : AC1 8) chain A residue 31 type sequence T description binding site for residue 947 A 401 source : AC1 9) chain A residue 34 type sequence L description binding site for residue 947 A 401 source : AC1 10) chain A residue 177 type sequence M description binding site for residue 947 A 401 source : AC1 11) chain A residue 179 type sequence C description binding site for residue 947 A 401 source : AC1 12) chain B residue 17 type sequence V description binding site for residue 947 B 401 source : AC2 13) chain B residue 20 type sequence E description binding site for residue 947 B 401 source : AC2 14) chain B residue 21 type sequence G description binding site for residue 947 B 401 source : AC2 15) chain B residue 22 type sequence R description binding site for residue 947 B 401 source : AC2 16) chain B residue 26 type sequence G description binding site for residue 947 B 401 source : AC2 17) chain B residue 27 type sequence T description binding site for residue 947 B 401 source : AC2 18) chain B residue 28 type sequence G description binding site for residue 947 B 401 source : AC2 19) chain B residue 29 type sequence E description binding site for residue 947 B 401 source : AC2 20) chain B residue 30 type sequence L description binding site for residue 947 B 401 source : AC2 21) chain B residue 31 type sequence T description binding site for residue 947 B 401 source : AC2 22) chain D residue 27 type sequence T description binding site for residue 947 B 401 source : AC2 23) chain A residue 27 type sequence T description binding site for residue 947 C 401 source : AC3 24) chain C residue 17 type sequence V description binding site for residue 947 C 401 source : AC3 25) chain C residue 20 type sequence E description binding site for residue 947 C 401 source : AC3 26) chain C residue 21 type sequence G description binding site for residue 947 C 401 source : AC3 27) chain C residue 22 type sequence R description binding site for residue 947 C 401 source : AC3 28) chain C residue 24 type sequence A description binding site for residue 947 C 401 source : AC3 29) chain C residue 26 type sequence G description binding site for residue 947 C 401 source : AC3 30) chain C residue 27 type sequence T description binding site for residue 947 C 401 source : AC3 31) chain C residue 28 type sequence G description binding site for residue 947 C 401 source : AC3 32) chain C residue 29 type sequence E description binding site for residue 947 C 401 source : AC3 33) chain C residue 30 type sequence L description binding site for residue 947 C 401 source : AC3 34) chain C residue 31 type sequence T description binding site for residue 947 C 401 source : AC3 35) chain D residue 17 type sequence V description binding site for residue 947 D 401 source : AC4 36) chain D residue 20 type sequence E description binding site for residue 947 D 401 source : AC4 37) chain D residue 21 type sequence G description binding site for residue 947 D 401 source : AC4 38) chain D residue 22 type sequence R description binding site for residue 947 D 401 source : AC4 39) chain D residue 24 type sequence A description binding site for residue 947 D 401 source : AC4 40) chain D residue 26 type sequence G description binding site for residue 947 D 401 source : AC4 41) chain D residue 27 type sequence T description binding site for residue 947 D 401 source : AC4 42) chain D residue 28 type sequence G description binding site for residue 947 D 401 source : AC4 43) chain D residue 29 type sequence E description binding site for residue 947 D 401 source : AC4 44) chain D residue 30 type sequence L description binding site for residue 947 D 401 source : AC4 45) chain D residue 31 type sequence T description binding site for residue 947 D 401 source : AC4 46) chain D residue 177 type sequence M description binding site for residue 947 D 401 source : AC4 47) chain E residue 17 type sequence V description binding site for residue 947 E 401 source : AC5 48) chain E residue 20 type sequence E description binding site for residue 947 E 401 source : AC5 49) chain E residue 21 type sequence G description binding site for residue 947 E 401 source : AC5 50) chain E residue 22 type sequence R description binding site for residue 947 E 401 source : AC5 51) chain E residue 26 type sequence G description binding site for residue 947 E 401 source : AC5 52) chain E residue 28 type sequence G description binding site for residue 947 E 401 source : AC5 53) chain E residue 29 type sequence E description binding site for residue 947 E 401 source : AC5 54) chain E residue 30 type sequence L description binding site for residue 947 E 401 source : AC5 55) chain E residue 31 type sequence T description binding site for residue 947 E 401 source : AC5 56) chain E residue 179 type sequence C description binding site for residue 947 E 401 source : AC5 57) chain F residue 17 type sequence V description binding site for residue 947 F 401 source : AC6 58) chain F residue 18 type sequence M description binding site for residue 947 F 401 source : AC6 59) chain F residue 20 type sequence E description binding site for residue 947 F 401 source : AC6 60) chain F residue 21 type sequence G description binding site for residue 947 F 401 source : AC6 61) chain F residue 22 type sequence R description binding site for residue 947 F 401 source : AC6 62) chain F residue 26 type sequence G description binding site for residue 947 F 401 source : AC6 63) chain F residue 27 type sequence T description binding site for residue 947 F 401 source : AC6 64) chain F residue 28 type sequence G description binding site for residue 947 F 401 source : AC6 65) chain F residue 29 type sequence E description binding site for residue 947 F 401 source : AC6 66) chain F residue 30 type sequence L description binding site for residue 947 F 401 source : AC6 67) chain F residue 31 type sequence T description binding site for residue 947 F 401 source : AC6 68) chain G residue 17 type sequence V description binding site for residue 947 G 401 source : AC7 69) chain G residue 18 type sequence M description binding site for residue 947 G 401 source : AC7 70) chain G residue 20 type sequence E description binding site for residue 947 G 401 source : AC7 71) chain G residue 21 type sequence G description binding site for residue 947 G 401 source : AC7 72) chain G residue 22 type sequence R description binding site for residue 947 G 401 source : AC7 73) chain G residue 26 type sequence G description binding site for residue 947 G 401 source : AC7 74) chain G residue 27 type sequence T description binding site for residue 947 G 401 source : AC7 75) chain G residue 28 type sequence G description binding site for residue 947 G 401 source : AC7 76) chain G residue 29 type sequence E description binding site for residue 947 G 401 source : AC7 77) chain G residue 30 type sequence L description binding site for residue 947 G 401 source : AC7 78) chain G residue 31 type sequence T description binding site for residue 947 G 401 source : AC7 79) chain G residue 177 type sequence M description binding site for residue 947 G 401 source : AC7 80) chain F residue 27 type sequence T description binding site for residue 947 H 401 source : AC8 81) chain H residue 17 type sequence V description binding site for residue 947 H 401 source : AC8 82) chain H residue 20 type sequence E description binding site for residue 947 H 401 source : AC8 83) chain H residue 21 type sequence G description binding site for residue 947 H 401 source : AC8 84) chain H residue 22 type sequence R description binding site for residue 947 H 401 source : AC8 85) chain H residue 26 type sequence G description binding site for residue 947 H 401 source : AC8 86) chain H residue 27 type sequence T description binding site for residue 947 H 401 source : AC8 87) chain H residue 28 type sequence G description binding site for residue 947 H 401 source : AC8 88) chain H residue 29 type sequence E description binding site for residue 947 H 401 source : AC8 89) chain H residue 30 type sequence L description binding site for residue 947 H 401 source : AC8 90) chain H residue 31 type sequence T description binding site for residue 947 H 401 source : AC8 91) chain E residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 92) chain E residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 93) chain E residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 94) chain E residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 95) chain E residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 96) chain E residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 97) chain F residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 98) chain F residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 99) chain F residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 100) chain F residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 101) chain F residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 102) chain F residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 103) chain G residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 104) chain G residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 105) chain G residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 106) chain G residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 107) chain G residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 108) chain G residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 109) chain H residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 110) chain H residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 111) chain H residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 112) chain H residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 113) chain H residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 114) chain H residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 115) chain A residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 116) chain D residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 117) chain A residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 118) chain A residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 119) chain B residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 120) chain B residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 121) chain B residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 122) chain B residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 123) chain B residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 124) chain C residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 125) chain C residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 126) chain C residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 127) chain C residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 128) chain C residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 129) chain C residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 130) chain D residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 131) chain D residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 132) chain D residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 133) chain D residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 134) chain D residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 135) chain B residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 136) chain A residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 137) chain A residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 138) chain A residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 139) chain E residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 140) chain E residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 141) chain E residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 142) chain E residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 143) chain F residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 144) chain F residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 145) chain F residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 146) chain F residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 147) chain G residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 148) chain G residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 149) chain G residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 150) chain G residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 151) chain H residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 152) chain H residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 153) chain H residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 154) chain H residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 155) chain D residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 156) chain D residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 157) chain C residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 158) chain C residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 159) chain C residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 160) chain D residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 161) chain D residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 162) chain A residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 163) chain A residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 164) chain A residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 165) chain B residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 166) chain B residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 167) chain B residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 168) chain B residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 169) chain C residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 170) chain A residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 171) chain E residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 172) chain E residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 173) chain E residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 174) chain F residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 175) chain F residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 176) chain F residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 177) chain G residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 178) chain G residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 179) chain G residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 180) chain H residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 181) chain H residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 182) chain H residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 183) chain A residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 184) chain A residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 185) chain A residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 186) chain D residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 187) chain D residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 188) chain D residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 189) chain C residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 190) chain B residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 191) chain B residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 192) chain B residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 193) chain C residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 194) chain C residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 195) chain E residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 196) chain F residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 197) chain G residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 198) chain H residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 199) chain A residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 200) chain B residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 201) chain C residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 202) chain D residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 203) chain E residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 204) chain F residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 205) chain F residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 206) chain G residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 207) chain G residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 208) chain H residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 209) chain H residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 210) chain E residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 211) chain A residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 212) chain A residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 213) chain B residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 214) chain D residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 215) chain B residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 216) chain C residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 217) chain C residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 218) chain D residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 219) chain E residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 220) chain F residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 221) chain G residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 222) chain H residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 223) chain A residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 224) chain B residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 225) chain C residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 226) chain D residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 227) chain A residue 273-285 type prosite sequence GKLRLLYECNPMA description FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA source prosite : PS00124

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