eF-site ID 9rub-AB PDB Code 9rub Chain A, B click to enlarge Title CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE COMPLEXED WITH ITS SUBSTRATE, RIBULOSE-1,5-BISPHOSPHATE Classification LYASE(CARBON-CARBON) Compound RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE Source null (RBL2_RHORU) Sequence A:  DQSSRYVNLALKEEDLIAGGEHVLCAYIMKPKAGYGYVAT AAHFAAESSTGTNVEVCTTDDFTRGVDALVYEVDEARELT KIAYPVALFDRNITDGKAMIASFLTLTMGNNQGMGDVEYA KMHDFYVPEAYRALFDGPSVNISALWKVLGRPEVDGGLVV GTIIKPKLGLRPKPFAEACHAFWLGGDFIKNDEPQGNQPF APLRDTIALVADAMRRAQDETGEAKLFSANITADDPFEII ARGEYVLETFGENASHVALLVDGYVAGAAAITTARRRFPD NFLHYHRAGHGAVTSPQSKRGYTAFVHCKMARLQGASGIH TGTMGFGKMEGESSDRAIAYMLTQDEAQGPFYRQSWGGMK ACTPIISGGMNALRMPGFFENLGNANVILTAGGGAFGHID GPVAGARSLRQAWQAWRDGVPVLDYAREHKELARAFESFP GDADQIYPGWRKALGVEDT B:  DQSSRYVNLALKEEDLIAGGEHVLCAYIMKPKAGYGYVAT AAHFAAESSTGTNVEVCTTDDFTRGVDALVYEVDEARELT KIAYPVALFDRNITDGKAMIASFLTLTMGNNQGMGDVEYA KMHDFYVPEAYRALFDGPSVNISALWKVLGRPEVDGGLVV GTIIKPKLGLRPKPFAEACHAFWLGGDFIKNDEPQGNQPF APLRDTIALVADAMRRAQDETGEAKLFSANITADDPFEII ARGEYVLETFGENASHVALLVDGYVAGAAAITTARRRFPD NFLHYHRAGHGAVTSPQSKRGYTAFVHCKMARLQGASGIH TGTMGFGKMEGESSDRAIAYMLTQDEAQGPFYRQSWGGMK ACTPIISGGMNALRMPGFFENLGNANVILTAGGGAFGHID GPVAGARSLRQAWQAWRDGVPVLDYAREHKELARAFESFP GDADQIYPGWRKALGVED Description (1)  RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGLUCOSE (RUBISCO) (E.C.4.1.1.39) COMPLEXED WITH CO2, MG++, AND SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE Functional site 1) chain A residue 191 type sequence K description ACTIVE SITE CHAIN A source : ACT 2) chain A residue 193 type sequence D description ACTIVE SITE CHAIN A source : ACT 3) chain A residue 194 type sequence E description ACTIVE SITE CHAIN A source : ACT 4) chain B residue 191 type sequence K description ACTIVE SITE CHAIN B source : BCT 5) chain B residue 193 type sequence D description ACTIVE SITE CHAIN B source : BCT 6) chain B residue 194 type sequence E description ACTIVE SITE CHAIN B source : BCT 7) chain A residue 164 type sequence I description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 8) chain A residue 193 type sequence D description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 9) chain A residue 321 type sequence H description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 10) chain A residue 366 type sequence I description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 11) chain A residue 368 type sequence S description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 12) chain A residue 392 type sequence A description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 13) chain A residue 393 type sequence G description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 14) chain B residue 111 type sequence N description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 15) chain B residue 164 type sequence I description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 16) chain B residue 287 type sequence H description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 17) chain B residue 321 type sequence H description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 18) chain B residue 322 type sequence T description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 19) chain B residue 368 type sequence S description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 20) chain B residue 369 type sequence G description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 21) chain B residue 391 type sequence T description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 22) chain B residue 392 type sequence A description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 23) chain B residue 393 type sequence G description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 24) chain A residue 193 type sequence D description BINDING SITE FOR RESIDUE MG A 500 source : AC3 25) chain B residue 193 type sequence D description BINDING SITE FOR RESIDUE MG B 500 source : AC4 26) chain B residue 194 type sequence E description BINDING SITE FOR RESIDUE MG B 500 source : AC4 27) chain A residue 164 type sequence I description BINDING SITE FOR RESIDUE FMT A 601 source : AC5 28) chain A residue 191 type sequence K description BINDING SITE FOR RESIDUE FMT A 601 source : AC5 29) chain A residue 192 type sequence N description BINDING SITE FOR RESIDUE FMT A 601 source : AC5 30) chain A residue 193 type sequence D description BINDING SITE FOR RESIDUE FMT A 601 source : AC5 31) chain B residue 191 type sequence K description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 32) chain B residue 193 type sequence D description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 33) chain B residue 194 type sequence E description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 34) chain B residue 287 type sequence H description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 35) chain B residue 321 type sequence H description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 36) chain A residue 186-194 type prosite sequence GGDFIKNDE description RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GgDFiKnDE source prosite : PS00157 37) chain A residue 166 type catalytic sequence K description 797 source MCSA : MCSA1 38) chain A residue 191 type catalytic sequence K description 797 source MCSA : MCSA1 39) chain A residue 192 type catalytic sequence N description 797 source MCSA : MCSA1 40) chain A residue 193 type catalytic sequence D description 797 source MCSA : MCSA1 41) chain A residue 194 type catalytic sequence E description 797 source MCSA : MCSA1 42) chain A residue 287 type catalytic sequence H description 797 source MCSA : MCSA1 43) chain A residue 321 type catalytic sequence H description 797 source MCSA : MCSA1 44) chain A residue 329 type catalytic sequence K description 797 source MCSA : MCSA1 45) chain B residue 166 type catalytic sequence K description 797 source MCSA : MCSA2 46) chain B residue 191 type catalytic sequence K description 797 source MCSA : MCSA2 47) chain B residue 192 type catalytic sequence N description 797 source MCSA : MCSA2 48) chain B residue 193 type catalytic sequence D description 797 source MCSA : MCSA2 49) chain B residue 194 type catalytic sequence E description 797 source MCSA : MCSA2 50) chain B residue 287 type catalytic sequence H description 797 source MCSA : MCSA2 51) chain B residue 321 type catalytic sequence H description 797 source MCSA : MCSA2 52) chain B residue 329 type catalytic sequence K description 797 source MCSA : MCSA2 53) chain B residue 166 type ACT_SITE sequence K description Proton acceptor source Swiss-Prot : SWS_FT_FI1 54) chain B residue 287 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 55) chain A residue 166 type ACT_SITE sequence K description Proton acceptor source Swiss-Prot : SWS_FT_FI1 56) chain A residue 287 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 57) chain A residue 191 type BINDING sequence K description via carbamate group => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 source Swiss-Prot : SWS_FT_FI4 58) chain B residue 191 type BINDING sequence K description via carbamate group => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 source Swiss-Prot : SWS_FT_FI4 59) chain A residue 194 type BINDING sequence E description BINDING => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 source Swiss-Prot : SWS_FT_FI5 60) chain B residue 193 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 194 type BINDING sequence E description BINDING => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 source Swiss-Prot : SWS_FT_FI5 62) chain A residue 193 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 source Swiss-Prot : SWS_FT_FI5 63) chain B residue 329 type SITE sequence K description Transition state stabilizer source Swiss-Prot : SWS_FT_FI6 64) chain A residue 329 type SITE sequence K description Transition state stabilizer source Swiss-Prot : SWS_FT_FI6 65) chain A residue 111 type BINDING sequence N description in homodimeric partner source Swiss-Prot : SWS_FT_FI2 66) chain B residue 111 type BINDING sequence N description in homodimeric partner source Swiss-Prot : SWS_FT_FI2 67) chain B residue 168 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 68) chain B residue 288 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 69) chain B residue 321 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 70) chain B residue 368 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 71) chain A residue 288 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 72) chain A residue 321 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 73) chain A residue 368 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 74) chain A residue 168 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 75) chain A residue 191 type MOD_RES sequence K description N6-carboxylysine => ECO:0000269|PubMed:1899197 source Swiss-Prot : SWS_FT_FI7 76) chain B residue 191 type MOD_RES sequence K description N6-carboxylysine => ECO:0000269|PubMed:1899197 source Swiss-Prot : SWS_FT_FI7

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