eF-site ID 4y24-AB PDB Code 4y24 Chain A, B click to enlarge Title Complex of human Galectin-1 and TD-139 Classification SUGAR BINDING PROTEIN Compound Galectin-1 Source Homo sapiens (Human) (LEG1_HUMAN) Sequence A:  CGLVASNLNLKPGECLRVRGEVAPDAKSFVLNLGKDSNNL CLHFNPRFNAHGDANTIVCNSKDGGAWGTEQREAVFPFQP GSVAEVCITFDQANLTVKLPDGYEFKFPNRLNLEAINYMA ADGDFKIKCVAFD B:  CGLVASNLNLKPGECLRVRGEVAPDAKSFVLNLGKDSNNL CLHFNPRFNAHGDANTIVCNSKDGGAWGTEQREAVFPFQP GSVAEVCITFDQANLTVKLPDGYEFKFPNRLNLEAINYMA ADGDFKIKCVAFD Description Functional site 1) chain A residue 29 type sequence S description binding site for residue TD2 A 201 source : AC1 2) chain A residue 30 type sequence F description binding site for residue TD2 A 201 source : AC1 3) chain A residue 31 type sequence V description binding site for residue TD2 A 201 source : AC1 4) chain A residue 44 type sequence H description binding site for residue TD2 A 201 source : AC1 5) chain A residue 48 type sequence R description binding site for residue TD2 A 201 source : AC1 6) chain A residue 54 type sequence D description binding site for residue TD2 A 201 source : AC1 7) chain A residue 61 type sequence N description binding site for residue TD2 A 201 source : AC1 8) chain A residue 68 type sequence W description binding site for residue TD2 A 201 source : AC1 9) chain A residue 71 type sequence E description binding site for residue TD2 A 201 source : AC1 10) chain A residue 73 type sequence R description binding site for residue TD2 A 201 source : AC1 11) chain A residue 124 type sequence G description binding site for residue TD2 A 201 source : AC1 12) chain B residue 70 type sequence T description binding site for residue TD2 A 201 source : AC1 13) chain B residue 109 type sequence P description binding site for residue TD2 A 201 source : AC1 14) chain B residue 111 type sequence R description binding site for residue TD2 A 201 source : AC1 15) chain A residue 72 type sequence Q description binding site for residue TD2 B 201 source : AC2 16) chain A residue 107 type sequence K description binding site for residue TD2 B 201 source : AC2 17) chain A residue 109 type sequence P description binding site for residue TD2 B 201 source : AC2 18) chain B residue 29 type sequence S description binding site for residue TD2 B 201 source : AC2 19) chain B residue 30 type sequence F description binding site for residue TD2 B 201 source : AC2 20) chain B residue 31 type sequence V description binding site for residue TD2 B 201 source : AC2 21) chain B residue 44 type sequence H description binding site for residue TD2 B 201 source : AC2 22) chain B residue 46 type sequence N description binding site for residue TD2 B 201 source : AC2 23) chain B residue 48 type sequence R description binding site for residue TD2 B 201 source : AC2 24) chain B residue 54 type sequence D description binding site for residue TD2 B 201 source : AC2 25) chain B residue 61 type sequence N description binding site for residue TD2 B 201 source : AC2 26) chain B residue 71 type sequence E description binding site for residue TD2 B 201 source : AC2 27) chain B residue 73 type sequence R description binding site for residue TD2 B 201 source : AC2 28) chain B residue 123 type sequence D description binding site for residue TD2 B 201 source : AC2 29) chain B residue 124 type sequence G description binding site for residue TD2 B 201 source : AC2 30) chain A residue 44 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 31) chain A residue 52 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 32) chain A residue 61 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 33) chain A residue 68 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 34) chain B residue 44 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 35) chain B residue 52 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 36) chain B residue 61 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 37) chain B residue 68 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 38) chain A residue 12 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P16045 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P16045 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 12 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P16045 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P16045 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 28 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 28 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 29 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 45) chain B residue 29 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P16045 source Swiss-Prot : SWS_FT_FI5 47) chain B 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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