eF-site ID 1ado-ABCD PDB Code 1ado Chain A, B, C, 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 A:  PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIA KRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFH ETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSA LAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEAS INLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENL KAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISN HAY B:  PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIA KRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFH ETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSA LAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEAS INLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENL KAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISN HAY C:  PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIA KRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFH ETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSA LAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEAS INLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENL KAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISN HAY D:  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 C residue 199 type sequence K description BINDING SITE FOR RESIDUE SO4 C 1326 source : AC1 3) chain C residue 202 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 1326 source : AC1 4) chain C residue 258 type sequence R description BINDING SITE FOR RESIDUE SO4 C 1326 source : AC1 5) chain A residue 12 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1261 source : AC2 6) chain D residue 199 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1261 source : AC2 7) chain D residue 202 type sequence Q description BINDING SITE FOR RESIDUE SO4 D 1261 source : AC2 8) chain D residue 258 type sequence R description BINDING SITE FOR RESIDUE SO4 D 1261 source : AC2 9) chain A residue 31 type sequence A description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 10) chain A residue 33 type sequence D description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 11) chain A residue 42 type sequence R description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 12) chain A residue 146 type sequence K description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 13) chain A residue 148 type sequence R description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 14) chain A residue 187 type sequence E description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 15) chain A residue 229 type sequence K description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 16) chain A residue 270 type sequence L description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 17) chain A residue 271 type sequence S description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 18) chain A residue 272 type sequence G description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 19) chain A residue 273 type sequence G description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 20) chain A residue 300 type sequence S description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 21) chain A residue 301 type sequence Y description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 22) chain A residue 302 type sequence G description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 23) chain A residue 303 type sequence R description BINDING SITE FOR RESIDUE 13P A 1104 source : AC3 24) chain B residue 270 type sequence L description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 25) chain B residue 271 type sequence S description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 26) chain B residue 272 type sequence G description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 27) chain B residue 273 type sequence G description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 28) chain B residue 300 type sequence S description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 29) chain B residue 301 type sequence Y description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 30) chain B residue 302 type sequence G description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 31) chain B residue 303 type sequence R description BINDING SITE FOR RESIDUE 13P B 1053 source : AC4 32) chain A residue 34 type catalytic sequence E description 222 source MCSA : MCSA1 33) chain A residue 147 type catalytic sequence W description 222 source MCSA : MCSA1 34) chain A residue 188 type catalytic sequence P description 222 source MCSA : MCSA1 35) chain A residue 190 type catalytic sequence I description 222 source MCSA : MCSA1 36) chain A residue 230 type catalytic sequence P description 222 source MCSA : MCSA1 37) chain A residue 301 type catalytic sequence Y description 222 source MCSA : MCSA1 38) chain B residue 34 type catalytic sequence E description 222 source MCSA : MCSA2 39) chain B residue 147 type catalytic sequence W description 222 source MCSA : MCSA2 40) chain B residue 188 type catalytic sequence P description 222 source MCSA : MCSA2 41) chain B residue 190 type catalytic sequence I description 222 source MCSA : MCSA2 42) chain B residue 230 type catalytic sequence P description 222 source MCSA : MCSA2 43) chain B residue 301 type catalytic sequence Y description 222 source MCSA : MCSA2 44) chain C residue 34 type catalytic sequence E description 222 source MCSA : MCSA3 45) chain C residue 147 type catalytic sequence W description 222 source MCSA : MCSA3 46) chain C residue 188 type catalytic sequence P description 222 source MCSA : MCSA3 47) chain C residue 190 type catalytic sequence I description 222 source MCSA : MCSA3 48) chain C residue 230 type catalytic sequence P description 222 source MCSA : MCSA3 49) chain C residue 301 type catalytic sequence Y description 222 source MCSA : MCSA3 50) chain D residue 34 type catalytic sequence E description 222 source MCSA : MCSA4 51) chain D residue 147 type catalytic sequence W description 222 source MCSA : MCSA4 52) chain D residue 188 type catalytic sequence P description 222 source MCSA : MCSA4 53) chain D residue 190 type catalytic sequence I description 222 source MCSA : MCSA4 54) chain D residue 230 type catalytic sequence P description 222 source MCSA : MCSA4 55) chain D residue 301 type catalytic sequence Y description 222 source MCSA : MCSA4 56) chain A residue 221-231 type prosite sequence IYLEGTLLKPN description ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN source prosite : PS00158 57) chain A residue 188 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI1 58) chain B residue 188 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI1 59) chain C residue 188 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI1 60) chain D residue 188 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 99 type MOD_RES sequence S description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 62) chain A residue 147 type MOD_RES sequence W description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 63) chain B residue 99 type MOD_RES sequence S description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 64) chain B residue 147 type MOD_RES sequence W description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 65) chain C residue 99 type MOD_RES sequence S description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 66) chain C residue 147 type MOD_RES sequence W description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 67) chain D residue 99 type MOD_RES sequence S description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 68) chain D residue 147 type MOD_RES sequence W description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI10 69) chain A residue 108 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 70) chain A residue 330 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 71) chain B residue 108 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 72) chain B residue 330 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 73) chain C residue 108 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 74) chain C residue 330 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 75) chain D residue 108 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 76) chain D residue 330 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI11 77) chain A residue 111 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 78) chain B residue 111 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 79) chain C residue 111 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 80) chain D residue 111 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 81) chain A residue 132 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI13 82) chain B residue 132 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI13 83) chain C residue 132 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI13 84) chain D residue 132 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI13 85) chain A residue 312 type MOD_RES sequence A description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 86) chain B residue 312 type MOD_RES sequence A description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 87) chain C residue 312 type MOD_RES sequence A description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 88) chain D residue 312 type MOD_RES sequence A description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI14 89) chain A residue 361 type MOD_RES sequence H description Deamidated asparagine; in form beta => ECO:0000269|PubMed:4857186 source Swiss-Prot : SWS_FT_FI15 90) 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 91) 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 92) 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 93) chain A 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 94) 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 95) 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 96) 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 97) chain A residue 230 type ACT_SITE sequence P description Schiff-base intermediate with dihydroxyacetone-P => ECO:0000269|PubMed:11779856 source Swiss-Prot : SWS_FT_FI2 98) 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 99) 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 100) 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 101) chain A residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 102) chain C residue 272 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 103) chain C residue 301 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 104) chain C residue 304 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 105) chain D residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 106) chain D residue 272 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 107) chain D residue 301 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 108) chain D residue 304 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 109) chain A residue 272 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 110) chain A residue 301 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 111) chain A residue 304 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 112) chain B residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 113) chain B residue 272 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 114) chain B residue 301 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 115) chain B residue 304 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 116) chain C residue 43 type BINDING sequence L description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 117) chain A residue 73 type SITE sequence I description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 118) chain A residue 108 type SITE sequence V description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 119) chain B residue 73 type SITE sequence I description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 120) chain B residue 108 type SITE sequence V description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 121) chain C residue 73 type SITE sequence I description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 122) chain C residue 108 type SITE sequence V description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 123) chain D residue 73 type SITE sequence I description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 124) chain D residue 108 type SITE sequence V description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 125) chain A residue 147 type SITE sequence W description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 126) chain B residue 147 type SITE sequence W description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 127) chain C residue 147 type SITE sequence W description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 128) chain D residue 147 type SITE sequence W description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 129) chain A 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 130) 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 131) 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 132) 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 133) chain A residue 9 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 134) chain B residue 9 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 135) chain C residue 9 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 136) chain D residue 9 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 137) chain A residue 36 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 138) chain C residue 39 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 139) chain C residue 46 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 140) chain C residue 272 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 141) chain D residue 36 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 142) chain D residue 39 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 143) chain D residue 46 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 144) chain D residue 272 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 145) chain A residue 39 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 146) chain A residue 46 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 147) chain A residue 272 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 148) chain B residue 36 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 149) chain B residue 39 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 150) chain B residue 46 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 151) chain B residue 272 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 152) chain C residue 36 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 153) chain A residue 42 type MOD_RES sequence R description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 154) chain B residue 42 type MOD_RES sequence R description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 155) chain C residue 42 type MOD_RES sequence R description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 156) 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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