eF-site ID 1geh-ABCDE PDB Code 1geh Chain A, B, C, D, E 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 null (RBL_PYRKO) Sequence A:  YVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESS TGTWTTLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAY PFHAFEEANLPGLLASIAGNIFGMKRVKGLRLEDLYFPEK LIREFDGPAFGIEGVRKMLEIKDRPIYGVVPKPKVGYSPE EFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIMAK IIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKH AMVDVVITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRN PYHGISMFVLAKLYRLIGIDQLHVGTAEGGKWDVIQNARI LRESHYKPDENDVFHLEQKFYSIKAAFPTSSGGLHPGNIQ PVIEALGTDIVLQLGGGTLGHPDGPAAGARAVRQAIDAIM QGIPLDEYAKTHKELARALEKWGHVTP B:  YVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESS TGTWTTLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAY PFHAFEEANLPGLLASIAGNIFGMKRVKGLRLEDLYFPEK LIREFDGPAFGIEGVRKMLEIKDRPIYGVVPKPKVGYSPE EFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIMAK IIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKH AMVDVVITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRN PYHGISMFVLAKLYRLIGIDQLHVGTAEGGKWDVIQNARI LRESHYKPDENDVFHLEQKFYSIKAAFPTSSGGLHPGNIQ PVIEALGTDIVLQLGGGTLGHPDGPAAGARAVRQAIDAIM QGIPLDEYAKTHKELARALEKWGHVTP C:  YVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESS TGTWTTLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAY PFHAFEEANLPGLLASIAGNIFGMKRVKGLRLEDLYFPEK LIREFDGPAFGIEGVRKMLEIKDRPIYGVVPKPKVGYSPE EFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIMAK IIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKH AMVDVVITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRN PYHGISMFVLAKLYRLIGIDQLHVGTAEGGKWDVIQNARI LRESHYKPDENDVFHLEQKFYSIKAAFPTSSGGLHPGNIQ PVIEALGTDIVLQLGGGTLGHPDGPAAGARAVRQAIDAIM QGIPLDEYAKTHKELARALEKWGHVTP D:  YVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESS TGTWTTLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAY PFHAFEEANLPGLLASIAGNIFGMKRVKGLRLEDLYFPEK LIREFDGPAFGIEGVRKMLEIKDRPIYGVVPKPKVGYSPE EFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIMAK IIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKH AMVDVVITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRN PYHGISMFVLAKLYRLIGIDQLHVGTAEGGKWDVIQNARI LRESHYKPDENDVFHLEQKFYSIKAAFPTSSGGLHPGNIQ PVIEALGTDIVLQLGGGTLGHPDGPAAGARAVRQAIDAIM QGIPLDEYAKTHKELARALEKWGHVTP E:  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 B residue 163 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1445 source : AC3 9) chain B residue 369 type sequence G description BINDING SITE FOR RESIDUE SO4 B 1445 source : AC3 10) chain B residue 389 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 1445 source : AC3 11) chain B residue 391 type sequence G description BINDING SITE FOR RESIDUE SO4 B 1445 source : AC3 12) chain B residue 392 type sequence G description BINDING SITE FOR RESIDUE SO4 B 1445 source : AC3 13) chain B residue 282 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1446 source : AC4 14) chain B residue 314 type sequence H description BINDING SITE FOR RESIDUE SO4 B 1446 source : AC4 15) chain C residue 163 type sequence K description BINDING SITE FOR RESIDUE SO4 C 2445 source : AC5 16) chain C residue 369 type sequence G description BINDING SITE FOR RESIDUE SO4 C 2445 source : AC5 17) chain C residue 389 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 2445 source : AC5 18) chain C residue 391 type sequence G description BINDING SITE FOR RESIDUE SO4 C 2445 source : AC5 19) chain C residue 392 type sequence G description BINDING SITE FOR RESIDUE SO4 C 2445 source : AC5 20) chain C residue 282 type sequence R description BINDING SITE FOR RESIDUE SO4 C 2446 source : AC6 21) chain C residue 314 type sequence H description BINDING SITE FOR RESIDUE SO4 C 2446 source : AC6 22) chain D residue 163 type sequence K description BINDING SITE FOR RESIDUE SO4 D 3445 source : AC7 23) chain D residue 369 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3445 source : AC7 24) chain D residue 389 type sequence Q description BINDING SITE FOR RESIDUE SO4 D 3445 source : AC7 25) chain D residue 391 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3445 source : AC7 26) chain D residue 392 type sequence G description BINDING SITE FOR RESIDUE SO4 D 3445 source : AC7 27) chain D residue 282 type sequence R description BINDING SITE FOR RESIDUE SO4 D 3446 source : AC8 28) chain D residue 314 type sequence H description BINDING SITE FOR RESIDUE SO4 D 3446 source : AC8 29) chain E residue 163 type sequence K description BINDING SITE FOR RESIDUE SO4 E 4445 source : AC9 30) chain E residue 369 type sequence G description BINDING SITE FOR RESIDUE SO4 E 4445 source : AC9 31) chain E residue 389 type sequence Q description BINDING SITE FOR RESIDUE SO4 E 4445 source : AC9 32) chain E residue 391 type sequence G description BINDING SITE FOR RESIDUE SO4 E 4445 source : AC9 33) chain E residue 392 type sequence G description BINDING SITE FOR RESIDUE SO4 E 4445 source : AC9 34) chain E residue 282 type sequence R description BINDING SITE FOR RESIDUE SO4 E 4446 source : BC1 35) chain E residue 314 type sequence H description BINDING SITE FOR RESIDUE SO4 E 4446 source : BC1 36) chain B residue 163 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 281 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 163 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 281 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 40) chain D residue 163 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 281 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 42) chain E residue 163 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 43) chain E residue 281 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 163 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 281 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 314 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 367 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 389 type BINDING sequence Q description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 389 type BINDING sequence Q description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 50) chain C residue 165 type BINDING sequence K description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 51) chain C residue 282 type BINDING sequence R description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 52) chain C residue 314 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 53) chain C residue 367 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 54) chain C residue 389 type BINDING sequence Q description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 55) chain D residue 165 type BINDING sequence K description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 56) chain D residue 282 type BINDING sequence R description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 57) chain D residue 314 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 58) chain D residue 367 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 59) chain D residue 389 type BINDING sequence Q description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 60) chain E residue 165 type BINDING sequence K description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 61) chain E residue 282 type BINDING sequence R description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 62) chain E residue 314 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 63) chain E residue 367 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 64) chain E residue 389 type BINDING sequence Q description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 65) chain B residue 165 type BINDING sequence K description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 66) chain B residue 282 type BINDING sequence R description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 67) chain B residue 314 type BINDING sequence H description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 367 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 165 type BINDING sequence K description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 70) chain A residue 282 type BINDING sequence R description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 71) chain B 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 72) chain C 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 73) chain D 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 74) chain E 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 75) 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 76) chain C residue 191 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 77) chain C residue 192 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 78) chain D residue 191 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 79) chain D residue 192 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 80) chain E residue 191 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 81) chain E residue 192 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 82) 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 83) 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 84) chain B residue 191 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 85) chain B residue 192 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 source Swiss-Prot : SWS_FT_FI4 86) chain B 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 87) chain C 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 88) chain D 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 89) chain E 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 90) 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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