eF-site ID 9rub-B PDB Code 9rub Chain 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 Rhodospirillum rubrum (RBL2_RHORU) Sequence 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 B residue 191 type sequence K description ACTIVE SITE CHAIN B source : BCT 2) chain B residue 193 type sequence D description ACTIVE SITE CHAIN B source : BCT 3) chain B residue 194 type sequence E description ACTIVE SITE CHAIN B source : BCT 4) chain B residue 111 type sequence N description BINDING SITE FOR RESIDUE RUB A 600 source : AC1 5) chain B residue 164 type sequence I description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 6) chain B residue 287 type sequence H description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 7) chain B residue 321 type sequence H description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 8) chain B residue 322 type sequence T description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 9) chain B residue 368 type sequence S description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 10) chain B residue 369 type sequence G description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 11) chain B residue 391 type sequence T description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 12) chain B residue 392 type sequence A description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 13) chain B residue 393 type sequence G description BINDING SITE FOR RESIDUE RUB B 700 source : AC2 14) chain B residue 193 type sequence D description BINDING SITE FOR RESIDUE MG B 500 source : AC4 15) chain B residue 194 type sequence E description BINDING SITE FOR RESIDUE MG B 500 source : AC4 16) chain B residue 191 type sequence K description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 17) chain B residue 193 type sequence D description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 18) chain B residue 194 type sequence E description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 19) chain B residue 287 type sequence H description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 20) chain B residue 321 type sequence H description BINDING SITE FOR RESIDUE FMT B 701 source : AC6 21) chain B residue 166 type catalytic sequence K description 797 source MCSA : MCSA2 22) chain B residue 191 type catalytic sequence K description 797 source MCSA : MCSA2 23) chain B residue 192 type catalytic sequence N description 797 source MCSA : MCSA2 24) chain B residue 193 type catalytic sequence D description 797 source MCSA : MCSA2 25) chain B residue 194 type catalytic sequence E description 797 source MCSA : MCSA2 26) chain B residue 287 type catalytic sequence H description 797 source MCSA : MCSA2 27) chain B residue 321 type catalytic sequence H description 797 source MCSA : MCSA2 28) chain B residue 329 type catalytic sequence K description 797 source MCSA : MCSA2 29) chain B residue 166 type ACT_SITE sequence K description Proton acceptor source Swiss-Prot : SWS_FT_FI1 30) chain B residue 287 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 31) chain B residue 111 type BINDING sequence N description in homodimeric partner source Swiss-Prot : SWS_FT_FI2 32) chain B residue 168 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 33) chain B residue 288 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 34) chain B residue 321 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 35) chain B residue 368 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 36) 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 37) chain B residue 193 type BINDING sequence D description BINDING => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 194 type BINDING sequence E description BINDING => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4 source Swiss-Prot : SWS_FT_FI5 39) chain B residue 329 type SITE sequence K description Transition state stabilizer source Swiss-Prot : SWS_FT_FI6 40) 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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