eF-site ID 1ub3-ABCD PDB Code 1ub3 Chain A, B, C, D click to enlarge Title Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8 Classification LYASE Compound Aldolase protein Source (Q7SIC8_THETH) Sequence A:  DLAAHIDHTLLKPTATLEEVAKAAEEALEYGFYGLCIPPS YVAWVRARYPHAPFRLVTVVGFPLGYQEKEVKALEAALAC ARGADEVDMVLHLGRAKAGDLDYLEAEVRAVREAVPQAVL KVILETGYFSPEEIARLAEAAIRGGADFLKTSTGFGPRGA SLEDVALLVRVAQGRAQVKAAGGIRDRETALRMLKAGASR LGTSSGVALVA B:  MDLAAHIDHTLLKPTATLEEVAKAAEEALEYGFYGLCIPP SYVAWVRARYPHAPFRLVTVVGFPLGYQEKEVKALEAALA CARGADEVDMVLHLGRAKAGDLDYLEAEVRAVREAVPQAV LKVILETGYFSPEEIARLAEAAIRGGADFLKTSTGFGPRG ASLEDVALLVRVAQGRAQVKAAGGIRDRETALRMLKAGAS RLGTSSGVALV C:  DLAAHIDHTLLKPTATLEEVAKAAEEALEYGFYGLCIPPS YVAWVRARYPHAPFRLVTVVGFPLGYQEKEVKALEAALAC ARGADEVDMVLHLGRAKAGDLDYLEAEVRAVREAVPQAVL KVILETGYFSPEEIARLAEAAIRGGADFLKTSTGFGPRGA SLEDVALLVRVAQGRAQVKAAGGIRDRETALRMLKAGASR LGTSSGVALV D:  DLAAHIDHTLLKPTATLEEVAKAAEEALEYGFYGLCIPPS YVAWVRARYPHAPFRLVTVVGFPLGYQEKEVKALEAALAC ARGADEVDMVLHLGRAKAGDLDYLEAEVRAVREAVPQAVL KVILETGYFSPEEIARLAEAAIRGGADFLKTSTGFGPRGA SLEDVALLVRVAQGRAQVKAAGGIRDRETALRMLKAGASR LGTSSGVALVA Description Functional site 1) chain A residue 12 type sequence L description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 2) chain A residue 37 type sequence C description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 3) chain A residue 60 type sequence V description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 4) chain A residue 151 type sequence K description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 5) chain A residue 154 type sequence T description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 6) chain A residue 155 type sequence G description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 7) chain A residue 182 type sequence A description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 8) chain A residue 183 type sequence G description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 9) chain A residue 184 type sequence G description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 10) chain A residue 186 type sequence R description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 11) chain A residue 203 type sequence G description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 12) chain A residue 204 type sequence T description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 13) chain A residue 205 type sequence S description BINDING SITE FOR RESIDUE HPD A 801 source : AC1 14) chain B residue 12 type sequence L description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 15) chain B residue 37 type sequence C description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 16) chain B residue 60 type sequence V description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 17) chain B residue 89 type sequence D description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 18) chain B residue 151 type sequence K description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 19) chain B residue 154 type sequence T description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 20) chain B residue 182 type sequence A description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 21) chain B residue 183 type sequence G description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 22) chain B residue 184 type sequence G description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 23) chain B residue 186 type sequence R description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 24) chain B residue 203 type sequence G description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 25) chain B residue 204 type sequence T description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 26) chain B residue 205 type sequence S description BINDING SITE FOR RESIDUE HPD B 802 source : AC2 27) chain C residue 12 type sequence L description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 28) chain C residue 37 type sequence C description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 29) chain C residue 60 type sequence V description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 30) chain C residue 151 type sequence K description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 31) chain C residue 154 type sequence T description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 32) chain C residue 155 type sequence G description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 33) chain C residue 182 type sequence A description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 34) chain C residue 183 type sequence G description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 35) chain C residue 184 type sequence G description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 36) chain C residue 186 type sequence R description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 37) chain C residue 203 type sequence G description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 38) chain C residue 204 type sequence T description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 39) chain C residue 205 type sequence S description BINDING SITE FOR RESIDUE HPD C 803 source : AC3 40) chain D residue 12 type sequence L description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 41) chain D residue 37 type sequence C description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 42) chain D residue 60 type sequence V description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 43) chain D residue 89 type sequence D description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 44) chain D residue 151 type sequence K description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 45) chain D residue 154 type sequence T description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 46) chain D residue 182 type sequence A description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 47) chain D residue 183 type sequence G description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 48) chain D residue 184 type sequence G description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 49) chain D residue 186 type sequence R description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 50) chain D residue 203 type sequence G description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 51) chain D residue 204 type sequence T description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 52) chain D residue 205 type sequence S description BINDING SITE FOR RESIDUE HPD D 804 source : AC4 53) chain A residue 89 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 180 type ACT_SITE sequence K description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 89 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 180 type ACT_SITE sequence K description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI1 57) chain C residue 89 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI1 58) chain C residue 180 type ACT_SITE sequence K description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI1 59) chain D residue 89 type ACT_SITE sequence D description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI1 60) chain D residue 180 type ACT_SITE sequence K description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 151 type ACT_SITE sequence K description Schiff-base intermediate with acetaldehyde => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 151 type ACT_SITE sequence K description Schiff-base intermediate with acetaldehyde => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI2 63) chain C residue 151 type ACT_SITE sequence K description Schiff-base intermediate with acetaldehyde => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI2 64) chain D residue 151 type ACT_SITE sequence K description Schiff-base intermediate with acetaldehyde => ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305|PubMed:15388928 source Swiss-Prot : SWS_FT_FI2

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