eF-site ID 1efh-A PDB Code 1efh Chain A click to enlarge Title CRYSTAL STRUCTURE OF THE HUMAN HYDROXYSTEROID SULFOTRANSFERASE IN THE PRESENCE OF PAP Classification TRANSFERASE Compound HYDROXYSTEROID SULFOTRANSFERASE Source (ST2A1_HUMAN) Sequence A:  DFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYP KSGTNWLAEILCLMHSKGDAKWIQSVPIWERSPWVESEIG YTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNP RDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSW FDHIHGWMPMREEKNFLLLSYEELKQDTGRTIEKICQFLG KTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVVDQL LRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRKLAAAL E Description Functional site 1) chain A residue 44 type sequence K description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 2) chain A residue 45 type sequence S description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 3) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 4) chain A residue 47 type sequence T description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 5) chain A residue 48 type sequence N description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 6) chain A residue 49 type sequence W description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 7) chain A residue 121 type sequence R description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 8) chain A residue 129 type sequence S description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 9) chain A residue 184 type sequence Y description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 10) chain A residue 218 type sequence S description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 11) chain A residue 219 type sequence S description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 12) chain A residue 220 type sequence F description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 13) chain A residue 223 type sequence M description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 14) chain A residue 245 type sequence L description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 15) chain A residue 246 type sequence L description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 16) chain A residue 247 type sequence R description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 17) chain A residue 248 type sequence K description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 18) chain A residue 249 type sequence G description BINDING SITE FOR RESIDUE A3P A 303 source : AC2 19) chain A residue 184 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI4 20) chain A residue 223 type BINDING sequence M description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI5 21) chain A residue 251 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 22) chain A residue 99 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:11988089, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1J99, ECO:0007744|PDB:1OV4 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 46 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10854859, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:1OV4, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI2 24) chain A residue 44 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10854859, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:1OV4, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI2 25) chain A residue 48 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10854859, ECO:0000269|PubMed:14573603, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:1OV4, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI2 26) chain A residue 49 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3 27) chain A residue 121 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3 28) chain A residue 129 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3 29) chain A residue 218 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3 30) chain A residue 247 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3 31) chain A residue 248 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3 32) chain A residue 249 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3 33) chain A residue 45 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3 34) chain A residue 47 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:1EFH, ECO:0007744|PDB:3F3Y, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI3

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