eF-site ID 5q0c-ABCDEFGH PDB Code 5q0c 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-[5-(4-methoxyphenyl)thiophen-2-yl]sulfonylurea and with fructose-2,6-diphosphate Classification HYDROLASE/HYDROLASE INHIBITOR Compound Fructose-1,6-bisphosphatase isozyme 2 Source (F16P2_HUMAN) Sequence A:  TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA VRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS SYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNID CLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALY GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGK IYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGS MVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEY LTCVQKNQ B:  TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA VRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS SYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNID CLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALY GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGK IYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGS MVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEY LTCVQKNQ C:  TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA VRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS SYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNID CLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALY GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGK IYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGS MVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEY LTCVQKNQ D:  TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA VRKAGLAHLYGIAGSVNVKLDVLSNSLVINMLQSSYSTCV LVSEENKDAIITAKEKRGKYVVCFDPLDGSSNIDCLASIG TIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALYGSATLV ALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNE GYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVH RTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGG LATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEYLTCVQK NQ E:  TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA VRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS SYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNID CLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALY GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGK IYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGS MVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEY LTCVQKNQ F:  TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA VRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS SYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNID CLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALY GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGK IYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGS MVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEY LTCVQKNQ G:  TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA VRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS SYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNID CLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALY GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGK IYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGS MVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEY LTCVQKNQ H:  TDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSA VRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMLQS SYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNID CLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALY GSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGK IYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGS MVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYI IEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEY LTCVQKNQ Description Functional site 1) chain A residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 2) chain C residue 28 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 3) chain C residue 113 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 4) chain C residue 141 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 6) chain D residue 28 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 7) chain D residue 113 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 8) chain D residue 141 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 9) chain E residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 10) chain E residue 28 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 11) chain E residue 113 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 28 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 13) chain E residue 141 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 14) chain F residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 15) chain F residue 28 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 16) chain F residue 113 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 17) chain F residue 141 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 18) chain G residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 19) chain G residue 28 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 20) chain G residue 113 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 21) chain G residue 141 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 22) chain H residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 113 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 24) chain H residue 28 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 25) chain H residue 113 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 26) chain H residue 141 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 141 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 28 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 113 type BINDING sequence K description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 141 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 32) chain C residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:22120740 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 69 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 281 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 35) chain B residue 69 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 36) chain B residue 98 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 37) chain B residue 119 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 38) chain B residue 121 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 39) chain B residue 122 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 40) chain B residue 213 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 41) chain B residue 245 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 42) chain B residue 265 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 43) chain B residue 275 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 44) chain A residue 98 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 45) chain B residue 281 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 46) chain C residue 69 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 47) chain C residue 98 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 48) chain C residue 119 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 49) chain C residue 121 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 50) chain C residue 122 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 51) chain C residue 213 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 52) chain C residue 245 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 53) chain C residue 265 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 54) chain C residue 275 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 55) chain A residue 119 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 56) chain C residue 281 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 57) chain D residue 98 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 58) chain D residue 119 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 59) chain D residue 121 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 60) chain D residue 122 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 61) chain D residue 213 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 62) chain D residue 245 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 63) chain D residue 265 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 64) chain D residue 275 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 65) chain A residue 121 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 66) chain D residue 281 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 67) chain E residue 69 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 68) chain E residue 98 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 69) chain E residue 119 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 70) chain E residue 121 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 71) chain E residue 122 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 72) chain E residue 213 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 73) chain E residue 245 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 74) chain E residue 265 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 75) chain E residue 275 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 76) chain A residue 122 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 77) chain E residue 281 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 78) chain F residue 69 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 79) chain F residue 98 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 80) chain F residue 119 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 81) chain F residue 121 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 82) chain F residue 122 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 83) chain F residue 213 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 84) chain F residue 245 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 85) chain F residue 265 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 86) chain F residue 275 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 87) chain A residue 213 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 88) chain F residue 281 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 89) chain G residue 69 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 90) chain G residue 98 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 91) chain G residue 119 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 92) chain G residue 121 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 93) chain G residue 122 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 94) chain G residue 213 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 95) chain G residue 245 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 96) chain G residue 265 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 97) chain G residue 275 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 98) chain A residue 245 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 99) chain G residue 281 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 100) chain H residue 69 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 101) chain H residue 98 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 102) chain H residue 119 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 103) chain H residue 121 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 104) chain H residue 122 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 105) chain H residue 213 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 106) chain H residue 245 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 107) chain H residue 265 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 108) chain H residue 275 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 109) chain A residue 265 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 110) chain H residue 281 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 111) chain A residue 275 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 112) chain A residue 33 type SITE sequence Q description Important for the conversion from active R-state to inactive T-state in the presence of AMP source Swiss-Prot : SWS_FT_FI3 113) chain B residue 33 type SITE sequence Q description Important for the conversion from active R-state to inactive T-state in the presence of AMP source Swiss-Prot : SWS_FT_FI3 114) chain C residue 33 type SITE sequence Q description Important for the conversion from active R-state to inactive T-state in the presence of AMP source Swiss-Prot : SWS_FT_FI3 115) chain D residue 33 type SITE sequence Q description Important for the conversion from active R-state to inactive T-state in the presence of AMP source Swiss-Prot : SWS_FT_FI3 116) chain E residue 33 type SITE sequence Q description Important for the conversion from active R-state to inactive T-state in the presence of AMP source Swiss-Prot : SWS_FT_FI3 117) chain F residue 33 type SITE sequence Q description Important for the conversion from active R-state to inactive T-state in the presence of AMP source Swiss-Prot : SWS_FT_FI3 118) chain G residue 33 type SITE sequence Q description Important for the conversion from active R-state to inactive T-state in the presence of AMP source Swiss-Prot : SWS_FT_FI3 119) chain H residue 33 type SITE sequence Q description Important for the conversion from active R-state to inactive T-state in the presence of AMP source Swiss-Prot : SWS_FT_FI3 120) chain A residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 121) chain E residue 219 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 122) chain F residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 123) chain F residue 219 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 124) chain G residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 125) chain G residue 219 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 126) chain H residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 127) chain H residue 219 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 128) chain A residue 219 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 129) chain B residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 130) chain B residue 219 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 131) chain C residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 132) chain C residue 219 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 133) chain D residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 134) chain D residue 219 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 135) chain E residue 216 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1N1 source Swiss-Prot : SWS_FT_FI4 136) chain A residue 274-286 type prosite sequence GKLRLLYECNPVA description FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPVA source prosite : PS00124

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