eF-site ID 1efh-B PDB Code 1efh Chain B 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 B:  DFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYP KSGTNWLAEILCLMHSKGDAKWIQSVPIWERSPWVESEIG YTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNP RDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSW FDHIHGWMPMREEKNFLLLSYEELKQDTGRTIEKICQFLG KTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVKAQL LRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRKLAAAL EH Description Functional site 1) chain B residue 44 type sequence K description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 2) chain B residue 45 type sequence S description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 3) chain B residue 46 type sequence G description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 4) chain B residue 47 type sequence T description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 5) chain B residue 48 type sequence N description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 6) chain B residue 49 type sequence W description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 7) chain B residue 121 type sequence R description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 8) chain B residue 129 type sequence S description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 9) chain B residue 184 type sequence Y description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 10) chain B residue 218 type sequence S description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 11) chain B residue 219 type sequence S description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 12) chain B residue 220 type sequence F description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 13) chain B residue 223 type sequence M description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 14) chain B residue 245 type sequence L description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 15) chain B residue 246 type sequence L description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 16) chain B residue 247 type sequence R description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 17) chain B residue 248 type sequence K description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 18) chain B residue 249 type sequence G description BINDING SITE FOR RESIDUE A3P B 302 source : AC1 19) chain B 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 20) chain B 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 21) chain B 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 22) chain B 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 23) chain B 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 24) chain B 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 25) chain B 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 26) chain B 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 27) chain B 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 28) chain B 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 29) chain B 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 30) chain B 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 31) chain B 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 32) chain B residue 184 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10854859, ECO:0007744|PDB:4IFB source Swiss-Prot : SWS_FT_FI4 33) chain B 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 34) chain B residue 251 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6

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