eF-site ID 1ado-D PDB Code 1ado Chain D click to enlarge Title FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE Classification LYASE Compound ALDOLASE Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence D:  PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIA KRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFH ETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSA LAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEAS INLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENL KAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISN HAY Description Functional site 1) chain D residue 199 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1261 source : AC2 2) chain D residue 202 type sequence Q description BINDING SITE FOR RESIDUE SO4 D 1261 source : AC2 3) chain D residue 258 type sequence R description BINDING SITE FOR RESIDUE SO4 D 1261 source : AC2 4) chain D residue 34 type catalytic sequence E description 222 source MCSA : MCSA4 5) chain D residue 147 type catalytic sequence W description 222 source MCSA : MCSA4 6) chain D residue 188 type catalytic sequence P description 222 source MCSA : MCSA4 7) chain D residue 190 type catalytic sequence I description 222 source MCSA : MCSA4 8) chain D residue 230 type catalytic sequence P description 222 source MCSA : MCSA4 9) chain D residue 301 type catalytic sequence Y description 222 source MCSA : MCSA4 10) chain D residue 188 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI1 11) chain D residue 99 type MOD_RES sequence S description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 12) chain D residue 147 type MOD_RES sequence W description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 13) chain D residue 108 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 14) chain D residue 330 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 15) chain D residue 111 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 16) chain D residue 132 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI13 17) chain D residue 312 type MOD_RES sequence A description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 18) chain D residue 361 type MOD_RES sequence H description Deamidated asparagine; in form beta => ECO:0000269|PubMed:4857186 source Swiss-Prot : SWS_FT_FI15 19) chain D residue 42 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI16 20) chain D residue 230 type ACT_SITE sequence P description Schiff-base intermediate with dihydroxyacetone-P => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI2 21) chain D residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 22) chain D residue 272 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 23) chain D residue 301 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 24) chain D residue 304 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 25) chain D residue 73 type SITE sequence I description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 26) chain D residue 108 type SITE sequence V description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 27) chain D residue 147 type SITE sequence W description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 28) chain D residue 362 type SITE sequence A description Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base source Swiss-Prot : SWS_FT_FI6 29) chain D residue 9 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 30) chain D residue 36 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 31) chain D residue 39 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 32) chain D residue 46 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 33) chain D residue 272 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 34) chain D residue 42 type MOD_RES sequence R description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9

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