eF-site ID 1ado-B PDB Code 1ado Chain B 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 B:  PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIA KRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFH ETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSA LAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEAS INLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENL KAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISN HAY Description Functional site 1) chain B residue 12 type sequence K description BINDING SITE FOR RESIDUE SO4 C 1326 source : AC1 2) chain B residue 270 type sequence L description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 3) chain B residue 271 type sequence S description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 4) chain B residue 272 type sequence G description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 5) chain B residue 273 type sequence G description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 6) chain B residue 300 type sequence S description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 7) chain B residue 301 type sequence Y description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 8) chain B residue 302 type sequence G description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 9) chain B residue 303 type sequence R description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 10) chain B residue 99 type MOD_RES sequence S description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 11) chain B residue 147 type MOD_RES sequence W description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 12) chain B residue 188 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI1 13) chain B residue 108 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 14) chain B residue 330 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 15) chain B residue 111 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 16) chain B residue 132 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI13 17) chain B residue 312 type MOD_RES sequence A description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 18) chain B residue 9 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 19) chain B residue 36 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 20) chain B residue 39 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 21) chain B residue 46 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 22) chain B residue 272 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 23) chain B residue 42 type MOD_RES sequence R description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 24) chain B residue 34 type catalytic sequence E description 222 source MCSA : MCSA2 25) chain B residue 147 type catalytic sequence W description 222 source MCSA : MCSA2 26) chain B residue 188 type catalytic sequence P description 222 source MCSA : MCSA2 27) chain B residue 190 type catalytic sequence I description 222 source MCSA : MCSA2 28) chain B residue 230 type catalytic sequence P description 222 source MCSA : MCSA2 29) chain B residue 301 type catalytic sequence Y description 222 source MCSA : MCSA2 30) chain B residue 361 type MOD_RES sequence H description Deamidated asparagine; in form beta => ECO:0000269|PubMed:4857186 source Swiss-Prot : SWS_FT_FI15 31) chain B 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 32) chain B residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 33) chain B residue 272 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 34) chain B residue 304 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 35) chain B residue 73 type SITE sequence I description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 36) chain B residue 108 type SITE sequence V description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 37) chain B residue 147 type SITE sequence W description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 38) chain B 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 39) chain B 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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