eF-site ID 1geh-A PDB Code 1geh Chain A click to enlarge Title CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE) Classification LYASE Compound RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE Source Pyrococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Thermococcus kodakaraensis (strain KOD1)) (RBL_PYRKO) Sequence A:  YVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESS TGTWTTLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAY PFHAFEEANLPGLLASIAGNIFGMKRVKGLRLEDLYFPEK LIREFDGPAFGIEGVRKMLEIKDRPIYGVVPKPKVGYSPE EFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIMAK IIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKH AMVDVVITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRN PYHGISMFVLAKLYRLIGIDQLHVGTAEGGKWDVIQNARI LRESHYKPDENDVFHLEQKFYSIKAAFPTSSGGLHPGNIQ PVIEALGTDIVLQLGGGTLGHPDGPAAGARAVRQAIDAIM QGIPLDEYAKTHKELARALEKWGHVTP Description Functional site 1) chain A residue 163 type sequence K description BINDING SITE FOR RESIDUE SO4 A 445 source : AC1 2) chain A residue 369 type sequence G description BINDING SITE FOR RESIDUE SO4 A 445 source : AC1 3) chain A residue 389 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 445 source : AC1 4) chain A residue 391 type sequence G description BINDING SITE FOR RESIDUE SO4 A 445 source : AC1 5) chain A residue 392 type sequence G description BINDING SITE FOR RESIDUE SO4 A 445 source : AC1 6) chain A residue 282 type sequence R description BINDING SITE FOR RESIDUE SO4 A 446 source : AC2 7) chain A residue 314 type sequence H description BINDING SITE FOR RESIDUE SO4 A 446 source : AC2 8) chain A residue 163 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 9) chain A residue 281 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 165 type BINDING sequence K description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 282 type BINDING sequence R description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 314 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 367 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 389 type BINDING sequence Q description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 189 type BINDING sequence K description via carbamate group => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 191 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 192 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 189 type MOD_RES sequence K description N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI6

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