eF-site ID 5mwx-A PDB Code 5mwx Chain A click to enlarge Title Galectin-1 in Complex with Ligand JB60 Classification TRANSFERASE Compound Galectin-1 Source (LEG1_HUMAN) Sequence A:  CGLVASNLNLKPGEXLRVRGEVAPDAKSFVLNLGKDSNNL CLHFNPRFNAHGDANTIVCNSKDGGAWGTEQREAVFPFQP GSVAEVXITFDQANLTVKLPDGYEFKFPNRLNLEAINYMA ADGDFKIKXVAFD Description (1)  Sucrose phosphorylase (E.C.2.4.1.7) Functional site 1) chain A residue 36 type sequence K description binding site for residue BME A 201 source : AC1 2) chain A residue 114 type sequence L description binding site for residue BME A 201 source : AC1 3) chain A residue 115 type sequence E description binding site for residue BME A 201 source : AC1 4) chain A residue 116 type sequence A description binding site for residue BME A 201 source : AC1 5) chain A residue 29 type sequence S description binding site for residue WYD A 202 source : AC2 6) chain A residue 44 type sequence H description binding site for residue WYD A 202 source : AC2 7) chain A residue 46 type sequence N description binding site for residue WYD A 202 source : AC2 8) chain A residue 48 type sequence R description binding site for residue WYD A 202 source : AC2 9) chain A residue 52 type sequence H description binding site for residue WYD A 202 source : AC2 10) chain A residue 61 type sequence N description binding site for residue WYD A 202 source : AC2 11) chain A residue 71 type sequence E description binding site for residue WYD A 202 source : AC2 12) chain A residue 73 type sequence R description binding site for residue WYD A 202 source : AC2 13) chain A residue 123 type sequence D description binding site for residue WYD A 202 source : AC2 14) chain A residue 124 type sequence G description binding site for residue WYD A 202 source : AC2 15) chain A residue 125 type sequence D description binding site for residue WYD A 202 source : AC2 16) chain A residue 101 type sequence P description binding site for residue SO4 B 201 source : AC3 17) chain A residue 102 type sequence D description binding site for residue SO4 B 201 source : AC3 18) chain A residue 72 type sequence Q description binding site for residue WYD B 202 source : AC4 19) chain A residue 93 type sequence Q description binding site for residue WYD B 202 source : AC4 20) chain A residue 113 type sequence N description binding site for residue WYD B 202 source : AC4 21) chain A residue 44 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 22) chain A residue 52 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 23) chain A residue 61 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 24) chain A residue 68 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 25) chain A residue 12 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P16045 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P16045 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 28 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 29 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P16045 source Swiss-Prot : SWS_FT_FI5

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