eF-site ID 1ado-C PDB Code 1ado Chain C 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 C:  PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIA KRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFH ETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSA LAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEAS INLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENL KAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISN HAY Description Functional site 1) chain C residue 199 type sequence K description BINDING SITE FOR RESIDUE SO4 C 1326 source : AC1 2) chain C residue 202 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 1326 source : AC1 3) chain C residue 258 type sequence R description BINDING SITE FOR RESIDUE SO4 C 1326 source : AC1 4) chain C residue 99 type MOD_RES sequence S description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 5) chain C residue 147 type MOD_RES sequence W description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 6) chain C residue 188 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI1 7) chain C residue 108 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 8) chain C residue 330 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 9) chain C residue 111 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 10) chain C residue 132 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI13 11) chain C residue 312 type MOD_RES sequence A description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 12) chain C residue 9 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 13) chain C residue 39 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 14) chain C residue 46 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 15) chain C residue 272 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 16) chain C residue 36 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 17) chain C residue 42 type MOD_RES sequence R description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 18) chain C residue 34 type catalytic sequence E description 222 source MCSA : MCSA3 19) chain C residue 147 type catalytic sequence W description 222 source MCSA : MCSA3 20) chain C residue 188 type catalytic sequence P description 222 source MCSA : MCSA3 21) chain C residue 190 type catalytic sequence I description 222 source MCSA : MCSA3 22) chain C residue 230 type catalytic sequence P description 222 source MCSA : MCSA3 23) chain C residue 301 type catalytic sequence Y description 222 source MCSA : MCSA3 24) chain C residue 361 type MOD_RES sequence H description Deamidated asparagine; in form beta => ECO:0000269|PubMed:4857186 source Swiss-Prot : SWS_FT_FI15 25) chain C 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 26) chain C residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 27) chain C residue 272 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 28) chain C residue 304 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 29) chain C residue 73 type SITE sequence I description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 30) chain C residue 108 type SITE sequence V description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 31) chain C residue 147 type SITE sequence W description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 32) chain C 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 33) chain C residue 230 type ACT_SITE sequence P description Schiff-base intermediate with dihydroxyacetone-P => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI2

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