eF-site ID 1svd-AM PDB Code 1svd Chain A, M click to enlarge Title The structure of Halothiobacillus neapolitanus RuBisCo Classification LYASE Compound ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit Source ORGANISM_SCIENTIFIC: Halothiobacillus neapolitanus; Sequence A:  TYWMPEYTPLDSDILACFKITPQPGVDREEAAAAVAAESS TGTWTTVWTDLLTDMDYYKGRAYRIEDVPGDDAAFYAFIA YPIDLFEEGSVVNVFTSLVGNVFGFKAVRGLRLEDVRFPL AYVKTCGGPPHGIQVERDKMNKYGRPLLGCTIKPKLGLSA KNYGRAVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVQ DATETAEAQTGERKGHYLNVTAPTPEEMYKRAEFAKEIGA PIIMHDYITGGFTANTGLAKWCQDNGVLLHIHRAMHAVID RNPNHGIHFRVLTKILRLSGGDHLHTGTVVGKLEGDRAST LGWIDLLRESFIPEDRSRGIFFDQDWGSMPGVFAVASGGI HVWHMPALVNIFGDDSVLQFGGGTLGHPWGNAAGAAANRV ALEACVEARNQGRDIEKEGKEILTAAAQHSPELKIAMETW KEIKF M:  EMQDYKQSLKYETFSYLPPMNAERIRAQIKYAIAQGWSPG IEHVEVKNSMNQYWYMWKLPFFGEQNVDNVLAEIEACRSA YPTHQVKLVAYDNYAQSLGLAFVVYRGN Description Functional site 1) chain A residue 288 type sequence R description BINDING SITE FOR RESIDUE SO4 A 474 source : AC1 2) chain A residue 320 type sequence H description BINDING SITE FOR RESIDUE SO4 A 474 source : AC1 3) chain A residue 372 type sequence S description BINDING SITE FOR RESIDUE SO4 A 474 source : AC1 4) chain A residue 374 type sequence G description BINDING SITE FOR RESIDUE SO4 A 475 source : AC2 5) chain A residue 396 type sequence G description BINDING SITE FOR RESIDUE SO4 A 475 source : AC2 6) chain A residue 397 type sequence G description BINDING SITE FOR RESIDUE SO4 A 475 source : AC2 7) chain A residue 156 type sequence N description BINDING SITE FOR RESIDUE GOL M 111 source : AC3 8) chain M residue 13 type sequence Y description BINDING SITE FOR RESIDUE GOL M 111 source : AC3 9) chain M residue 51 type sequence S description BINDING SITE FOR RESIDUE GOL M 111 source : AC3 10) chain M residue 89 type sequence K description BINDING SITE FOR RESIDUE GOL M 111 source : AC3 11) chain A residue 189-197 type prosite sequence GLDFTKDDE description RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE source prosite : PS00157 12) chain A residue 168 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 287 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 116 type BINDING sequence N description in homodimeric partner => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 166 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 170 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 196 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 197 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 288 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 320 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 372 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 194 type BINDING sequence K description via carbamate group => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 327 type SITE sequence K description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 194 type MOD_RES sequence K description N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01338 source Swiss-Prot : SWS_FT_FI6

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