eF-site ID 3a9c-ABCDEF PDB Code 3a9c Chain A, B, C, D, E, F click to enlarge Title Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakaraensis KOD1 in complex with ribulose-1,5-bisphosphate Classification ISOMERASE Compound Translation initiation factor eIF-2B, delta subunit Source Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (Q5JFM9_PYRKO) Sequence A:  VVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSKA TNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGKI AYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAKR IEDGDVIMTHXHSKAAISVMKTAWEQGKDIKVIVTETRPK WQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGAD SITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHPE TMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDVT PPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWED B:  HIEGRHMAVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQ LQAEKSKATNVDEFWKEMKQAAKILFETRPTAVSLPNALR YVMHRGKIAYSSGADLEQLRFVIINAAKEFIHNSEKALER IGEFGAKRIEDGDVIMTHXHSKAAISVMKTAWEQGKDIKV IVTETRPKWQGKITAKELASYGIPVIYVVDSAARHYMKMT DKVVMGADSITVNGAVINKIGTALIALTAKEHRVWTMIAA ETYKFHPETMLVEIEMRDPTEVIPEDELKTWPKNIEVWNP AFDVTPPEYVDVIITERGIIPPYAAIDILREEFGWALKYT EPWED C:  AVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSK ATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGK IAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAK RIEDGDVIMTHXHSKAAISVMKTAWEQGKDIKVIVTETRP KWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGA DSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHP ETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDV TPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWE D D:  MAVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKS KATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRG KIAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGA KRIEDGDVIMTHXHSKAAISVMKTAWEQGKDIKVIVTETR PKWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMG ADSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFH PETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFD VTPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPW ED E:  AVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKSK ATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRGK IAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGAK RIEDGDVIMTHXHSKAAISVMKTAWEQGKDIKVIVTETRP KWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMGA DSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFHP ETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFDV TPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPWE D F:  MAVVKEVLEIAEKIKNMEIRGAGKIARSAAYALQLQAEKS KATNVDEFWKEMKQAAKILFETRPTAVSLPNALRYVMHRG KIAYSSGADLEQLRFVIINAAKEFIHNSEKALERIGEFGA KRIEDGDVIMTHXHSKAAISVMKTAWEQGKDIKVIVTETR PKWQGKITAKELASYGIPVIYVVDSAARHYMKMTDKVVMG ADSITVNGAVINKIGTALIALTAKEHRVWTMIAAETYKFH PETMLGQLVEIEMRDPTEVIPEDELKTWPKNIEVWNPAFD VTPPEYVDVIITERGIIPPYAAIDILREEFGWALKYTEPW ED Description Functional site 1) chain A residue 133 type sequence X description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 2) chain A residue 135 type sequence S description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 3) chain A residue 136 type sequence K description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 4) chain A residue 137 type sequence A description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 5) chain A residue 201 type sequence A description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 6) chain A residue 212 type sequence N description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 7) chain A residue 213 type sequence K description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 8) chain A residue 238 type sequence K description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 9) chain A residue 254 type sequence R description BINDING SITE FOR RESIDUE RUB A 401 source : AC1 10) chain A residue 224 type sequence K description BINDING SITE FOR RESIDUE PEG A 402 source : AC2 11) chain A residue 228 type sequence V description BINDING SITE FOR RESIDUE PEG A 402 source : AC2 12) chain A residue 285 type sequence E description BINDING SITE FOR RESIDUE PEG A 402 source : AC2 13) chain A residue 288 type sequence D description BINDING SITE FOR RESIDUE PEG A 402 source : AC2 14) chain A residue 304 type sequence D description BINDING SITE FOR RESIDUE MG A 411 source : AC3 15) chain E residue 304 type sequence D description BINDING SITE FOR RESIDUE MG A 411 source : AC3 16) chain B residue 133 type sequence X description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 17) chain B residue 135 type sequence S description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 18) chain B residue 136 type sequence K description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 19) chain B residue 137 type sequence A description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 20) chain B residue 201 type sequence A description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 21) chain B residue 202 type sequence D description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 22) chain B residue 212 type sequence N description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 23) chain B residue 213 type sequence K description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 24) chain B residue 238 type sequence K description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 25) chain B residue 254 type sequence R description BINDING SITE FOR RESIDUE RUB B 401 source : AC4 26) chain B residue 223 type sequence A description BINDING SITE FOR RESIDUE PEG B 402 source : AC5 27) chain B residue 224 type sequence K description BINDING SITE FOR RESIDUE PEG B 402 source : AC5 28) chain B residue 227 type sequence R description BINDING SITE FOR RESIDUE PEG B 402 source : AC5 29) chain B residue 228 type sequence V description BINDING SITE FOR RESIDUE PEG B 402 source : AC5 30) chain B residue 230 type sequence T description BINDING SITE FOR RESIDUE PEG B 402 source : AC5 31) chain B residue 286 type sequence Y description BINDING SITE FOR RESIDUE PEG B 402 source : AC5 32) chain B residue 288 type sequence D description BINDING SITE FOR RESIDUE PEG B 402 source : AC5 33) chain B residue 304 type sequence D description BINDING SITE FOR RESIDUE MG B 411 source : AC6 34) chain D residue 304 type sequence D description BINDING SITE FOR RESIDUE MG B 411 source : AC6 35) chain C residue 133 type sequence X description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 36) chain C residue 135 type sequence S description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 37) chain C residue 136 type sequence K description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 38) chain C residue 137 type sequence A description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 39) chain C residue 164 type sequence Q description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 40) chain C residue 201 type sequence A description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 41) chain C residue 212 type sequence N description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 42) chain C residue 213 type sequence K description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 43) chain C residue 238 type sequence K description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 44) chain C residue 254 type sequence R description BINDING SITE FOR RESIDUE RUB C 401 source : AC7 45) chain C residue 224 type sequence K description BINDING SITE FOR RESIDUE PEG C 402 source : AC8 46) chain C residue 228 type sequence V description BINDING SITE FOR RESIDUE PEG C 402 source : AC8 47) chain C residue 285 type sequence E description BINDING SITE FOR RESIDUE PEG C 402 source : AC8 48) chain C residue 286 type sequence Y description BINDING SITE FOR RESIDUE PEG C 402 source : AC8 49) chain C residue 288 type sequence D description BINDING SITE FOR RESIDUE PEG C 402 source : AC8 50) chain D residue 133 type sequence X description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 51) chain D residue 135 type sequence S description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 52) chain D residue 136 type sequence K description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 53) chain D residue 137 type sequence A description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 54) chain D residue 164 type sequence Q description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 55) chain D residue 201 type sequence A description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 56) chain D residue 212 type sequence N description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 57) chain D residue 213 type sequence K description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 58) chain D residue 238 type sequence K description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 59) chain D residue 254 type sequence R description BINDING SITE FOR RESIDUE RUB D 401 source : AC9 60) chain D residue 224 type sequence K description BINDING SITE FOR RESIDUE PEG D 402 source : BC1 61) chain D residue 227 type sequence R description BINDING SITE FOR RESIDUE PEG D 402 source : BC1 62) chain D residue 228 type sequence V description BINDING SITE FOR RESIDUE PEG D 402 source : BC1 63) chain D residue 286 type sequence Y description BINDING SITE FOR RESIDUE PEG D 402 source : BC1 64) chain D residue 288 type sequence D description BINDING SITE FOR RESIDUE PEG D 402 source : BC1 65) chain E residue 133 type sequence X description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 66) chain E residue 135 type sequence S description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 67) chain E residue 136 type sequence K description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 68) chain E residue 137 type sequence A description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 69) chain E residue 164 type sequence Q description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 70) chain E residue 201 type sequence A description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 71) chain E residue 212 type sequence N description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 72) chain E residue 213 type sequence K description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 73) chain E residue 238 type sequence K description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 74) chain E residue 254 type sequence R description BINDING SITE FOR RESIDUE RUB E 401 source : BC2 75) chain E residue 224 type sequence K description BINDING SITE FOR RESIDUE PEG E 402 source : BC3 76) chain E residue 227 type sequence R description BINDING SITE FOR RESIDUE PEG E 402 source : BC3 77) chain E residue 228 type sequence V description BINDING SITE FOR RESIDUE PEG E 402 source : BC3 78) chain E residue 229 type sequence W description BINDING SITE FOR RESIDUE PEG E 402 source : BC3 79) chain E residue 288 type sequence D description BINDING SITE FOR RESIDUE PEG E 402 source : BC3 80) chain F residue 133 type sequence X description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 81) chain F residue 135 type sequence S description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 82) chain F residue 136 type sequence K description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 83) chain F residue 137 type sequence A description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 84) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 85) chain F residue 212 type sequence N description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 86) chain F residue 213 type sequence K description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 87) chain F residue 238 type sequence K description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 88) chain F residue 254 type sequence R description BINDING SITE FOR RESIDUE RUB F 401 source : BC4 89) chain F residue 224 type sequence K description BINDING SITE FOR RESIDUE PEG F 402 source : BC5 90) chain F residue 227 type sequence R description BINDING SITE FOR RESIDUE PEG F 402 source : BC5 91) chain F residue 228 type sequence V description BINDING SITE FOR RESIDUE PEG F 402 source : BC5 92) chain F residue 230 type sequence T description BINDING SITE FOR RESIDUE PEG F 402 source : BC5 93) chain F residue 288 type sequence D description BINDING SITE FOR RESIDUE PEG F 402 source : BC5 94) chain A residue 227 type SITE sequence R description Plays a key role in hexamerization source Swiss-Prot : SWS_FT_FI5 95) chain B residue 227 type SITE sequence R description Plays a key role in hexamerization source Swiss-Prot : SWS_FT_FI5 96) chain C residue 227 type SITE sequence R description Plays a key role in hexamerization source Swiss-Prot : SWS_FT_FI5 97) chain D residue 227 type SITE sequence R description Plays a key role in hexamerization source Swiss-Prot : SWS_FT_FI5 98) chain E residue 227 type SITE sequence R description Plays a key role in hexamerization source Swiss-Prot : SWS_FT_FI5 99) chain F residue 227 type SITE sequence R description Plays a key role in hexamerization source Swiss-Prot : SWS_FT_FI5 100) chain A residue 63 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 101) chain E residue 238 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 102) chain F residue 63 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 103) chain F residue 238 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 104) chain A residue 238 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 105) chain B residue 63 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 106) chain B residue 238 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 107) chain C residue 63 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 108) chain C residue 238 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 109) chain D residue 63 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 110) chain D residue 238 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 111) chain E residue 63 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI4 112) chain A residue 133 type ACT_SITE sequence X description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI1 113) chain B residue 133 type ACT_SITE sequence X description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI1 114) chain C residue 133 type ACT_SITE sequence X description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI1 115) chain D residue 133 type ACT_SITE sequence X description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI1 116) chain E residue 133 type ACT_SITE sequence X description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI1 117) chain F residue 133 type ACT_SITE sequence X description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI1 118) chain A residue 202 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI2 119) chain B residue 202 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI2 120) chain C residue 202 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI2 121) chain D residue 202 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI2 122) chain E residue 202 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI2 123) chain F residue 202 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 source Swiss-Prot : SWS_FT_FI2 124) chain A residue 20 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 125) chain D residue 20 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 126) chain D residue 135 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 127) chain D residue 212 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 128) chain E residue 20 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 129) chain E residue 135 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 130) chain E residue 212 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 131) chain F residue 20 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 132) chain F residue 135 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 133) chain F residue 212 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 134) chain A residue 135 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 135) chain A residue 212 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 136) chain B residue 20 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 137) chain B residue 135 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 138) chain B residue 212 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 139) chain C residue 20 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 140) chain C residue 135 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3 141) chain C residue 212 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_02230 source Swiss-Prot : SWS_FT_FI3

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