eF-site ID 2c1z-A PDB Code 2c1z Chain A click to enlarge Title Structure and activity of a flavonoid 3-O glucosyltransferase reveals the basis for plant natural product modification Classification TRANSFERASE Compound UDP-GLUCOSE FLAVONOID 3-O GLYCOSYLTRANSFERASE Source (O22304_VITVI) Sequence A:  TNPHVAVLAFPFSTHAAPLLAVVRRLAAAAPHAVFSFFST SQSNASIFHDHTMQCNIKSYDISDGVPEGYVFAGRPQEDI ELFTRAAPESFRQGMVMAVAETGRPVSCLVADAFIWFAAD MAAEMGVAWLPFWTAGPNSLSTHVYIDEIREKIGVSGIQG REDELLNFIPGMSKVRFRDLQEGIVFGNLNSLFSRMLHRM GQVLPKATAVFINSFEELDDSLTNDLKSKLKTYLNIGPFN LITGCLQWLKERKPTSVVYISFGTVTTPPPAEVVALSEAL EASRVPFIWSLRDKARVHLPEGFLEKTRGYGMVVPWAPQA EVLAHEAVGAFVTHCGWNSLWESVAGGVPLICRPFFGDQR LNGRMVEDVLEIGVRIEGGVFTKSGLMSCFDQILSQEKGK KLRENLRALRETADRAVGPKGSSTENFITLVDLVSKPKD Description (1)  UDP-GLUCOSE FLAVONOID 3-O GLYCOSYLTRANSFERASE (E.C.2.4.1.91) Functional site 1) chain A residue 18 type sequence S description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 2) chain A residue 20 type sequence H description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 3) chain A residue 84 type sequence Q description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 4) chain A residue 87 type sequence I description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 5) chain A residue 121 type sequence F description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 6) chain A residue 146 type sequence S description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 7) chain A residue 150 type sequence H description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 8) chain A residue 188 type sequence Q description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 9) chain A residue 200 type sequence F description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 10) chain A residue 372 type sequence F description BINDING SITE FOR RESIDUE KMP A1456 source : AC1 11) chain A residue 18 type sequence S description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 12) chain A residue 19 type sequence T description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 13) chain A residue 20 type sequence H description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 14) chain A residue 141 type sequence T description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 15) chain A residue 275 type sequence Y description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 16) chain A residue 277 type sequence S description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 17) chain A residue 280 type sequence T description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 18) chain A residue 306 type sequence S description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 19) chain A residue 332 type sequence W description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 20) chain A residue 333 type sequence A description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 21) chain A residue 335 type sequence Q description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 22) chain A residue 350 type sequence H description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 23) chain A residue 352 type sequence G description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 24) chain A residue 353 type sequence W description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 25) chain A residue 354 type sequence N description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 26) chain A residue 355 type sequence S description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 27) chain A residue 358 type sequence E description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 28) chain A residue 372 type sequence F description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 29) chain A residue 374 type sequence D description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 30) chain A residue 375 type sequence Q description BINDING SITE FOR RESIDUE U2F A1457 source : AC2 31) chain A residue 119 type ACT_SITE sequence D description Charge relay => ECO:0000250|UniProtKB:A0A0A1HA03 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 18 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16482224, ECO:0007744|PDB:2C9Z source Swiss-Prot : SWS_FT_FI3 33) chain A residue 84 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16482224, ECO:0007744|PDB:2C9Z source Swiss-Prot : SWS_FT_FI3 34) chain A residue 150 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16482224, ECO:0007744|PDB:2C9Z source Swiss-Prot : SWS_FT_FI3 35) chain A residue 188 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16482224, ECO:0007744|PDB:2C9Z source Swiss-Prot : SWS_FT_FI3 36) chain A residue 373 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16482224, ECO:0007744|PDB:2C9Z source Swiss-Prot : SWS_FT_FI3 37) chain A residue 19 type BINDING sequence T description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 38) chain A residue 141 type BINDING sequence T description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 39) chain A residue 280 type BINDING sequence T description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 40) chain A residue 306 type BINDING sequence S description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 41) chain A residue 332 type BINDING sequence W description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 42) chain A residue 333 type BINDING sequence A description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 43) chain A residue 350 type BINDING sequence H description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 44) chain A residue 353 type BINDING sequence W description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 45) chain A residue 354 type BINDING sequence N description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 46) chain A residue 355 type BINDING sequence S description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 47) chain A residue 358 type BINDING sequence E description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 48) chain A residue 374 type BINDING sequence D description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 49) chain A residue 375 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI4 50) chain A residue 20 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16482224, ECO:0007744|PDB:2C1Z source Swiss-Prot : SWS_FT_FI5 51) chain A residue 332-375 type prosite sequence WAPQAEVLAHEAVGAFVTHCGWNSLWESVAGGVPLICRPF FGDQ description UDPGT UDP-glycosyltransferases signature. WapQaeVLaheavgAFVTHCGwnSlweSVaggv.PLicrPffgDQ source prosite : PS00375 52) chain A residue 20 type ACT_SITE sequence H description Proton acceptor => ECO:0000250|UniProtKB:A0A0A1HA03 source Swiss-Prot : SWS_FT_FI1

Display surface Download Links