eF-site ID 5wmh-ABCDEF PDB Code 5wmh Chain A, B, C, D, E, F click to enlarge Title Arabidopsis thaliana prephenate aminotransferase Classification TRANSFERASE Compound Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase Source (PAT_ARATH) Sequence A:  SLSPRVQSLKPSKTMVITDLAATLVQSGVPVIRLAAGEPD FDTPKVVAEAGINAIREGFTRYTLNAGITELREAICRKLK EENGLSYAPDQILVSNGAKQSLLQAVLAVCSPGDEVIIPA PYWVSYTEQARLADATPVVIPTKISNNFLLDPKDLESKLT EKSRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPRLLVL SDEIYEHIIYAPATHTSFASLPDMYERTLTVNGFSKAFAM TGWRLGYLAGPKHIVAACSKLQGQVSSGASSIAQKAGVAA LGLGKAGGETVAEMVKAYRERRDFLVKSLGDIKGVKISEP QGAFYLFIDFSAYYGSEAEGFGLINDSSSLALYFLDKFQV AMVPGDAFGDDSCIRISYATSLDVLQAAVEKIRKALEPL B:  SLSPRVQSLKPSKTMVITDLAATLVQSGVPVIRLAAGEPD FDTPKVVAEAGINAIREGFTRYTLNAGITELREAICRKLK EENGLSYAPDQILVSNGAKQSLLQAVLAVCSPGDEVIIPA PYWVSYTEQARLADATPVVIPTKISNNFLLDPKDLESKLT EKSRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPRLLVL SDEIYEHIIYAPATHTSFASLPDMYERTLTVNGFSKAFAM TGWRLGYLAGPKHIVAACSKLQGQVSSGASSIAQKAGVAA LGLGKAGGETVAEMVKAYRERRDFLVKSLGDIKGVKISEP QGAFYLFIDFSAYYGSEAEGFGLINDSSSLALYFLDKFQV AMVPGDAFGDDSCIRISYATSLDVLQAAVEKIRKALEPL C:  DMSLSPRVQSLKPSKTMVITDLAATLVQSGVPVIRLAAGE PDFDTPKVVAEAGINAIREGFTRYTLNAGITELREAICRK LKEENGLSYAPDQILVSNGAKQSLLQAVLAVCSPGDEVII PAPYWVSYTEQARLADATPVVIPTKISNNFLLDPKDLESK LTEKSRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPRLL VLSDEIYEHIIYAPATHTSFASLPDMYERTLTVNGFSKAF AMTGWRLGYLAGPKHIVAACSKLQGQVSSGASSIAQKAGV AALGLGKAGGETVAEMVKAYRERRDFLVKSLGDIKGVKIS EPQGAFYLFIDFSAYYGSEAEGFGLINDSSSLALYFLDKF QVAMVPGDAFGDDSCIRISYATSLDVLQAAVEKIRKALEP L D:  MSLSPRVQSLKPSKTMVITDLAATLVQSGVPVIRLAAGEP DFDTPKVVAEAGINAIREGFTRYTLNAGITELREAICRKL KEENGLSYAPDQILVSNGAKQSLLQAVLAVCSPGDEVIIP APYWVSYTEQARLADATPVVIPTKISNNFLLDPKDLESKL TEKSRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPRLLV LSDEIYEHIIYAPATHTSFASLPDMYERTLTVNGFSKAFA MTGWRLGYLAGPKHIVAACSKLQGQVSSGASSIAQKAGVA ALGLGKAGGETVAEMVKAYRERRDFLVKSLGDIKGVKISE PQGAFYLFIDFSAYYGSEAEGFGLINDSSSLALYFLDKFQ VAMVPGDAFGDDSCIRISYATSLDVLQAAVEKIRKALEPL E:  SLSPRVQSLKPSKTMVITDLAATLVQSGVPVIRLAAGEPD FDTPKVVAEAGINAIREGFTRYTLNAGITELREAICRKLK EENGLSYAPDQILVSNGAKQSLLQAVLAVCSPGDEVIIPA PYWVSYTEQARLADATPVVIPTKISNNFLLDPKDLESKLT EKSRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPRLLVL SDEIYEHIIYAPATHTSFASLPDMYERTLTVNGFSKAFAM TGWRLGYLAGPKHIVAACSKLQGQVSSGASSIAQKAGVAA LGLGKAGGETVAEMVKAYRERRDFLVKSLGDIKGVKISEP QGAFYLFIDFSAYYGSEAEGFGLINDSSSLALYFLDKFQV AMVPGDAFGDDSCIRISYATSLDVLQAAVEKIRKALEPL F:  DMSLSPRVQSLTMVITDLAATLVQSGVPVIRLAAGEPDFD TPKVVAEAGINAIREGFTRYTLNAGITELREAICRKLKEE NGLSYAPDQILVSNGAKQSLLQAVLAVCSPGDEVIIPAPY WVSYTEQARLADATPVVIPTKISNNFLLDPKDLESKLTEK SRLLILCSPSNPTGSVYPKSLLEEIARIIAKHPRLLVLSD EIYEHIIYAPATHTSFASLPDMYERTLTVNGFSKAFAMTG WRLGYLAGPKHIVAACSKLQGQVSSGASSIAQKAGVAALG LGKAGGETVAEMVKAYRERRDFLVKSLGDIKGVKISEPQG AFYLFIDFSAYYGSEAEGFGLINDSSSLALYFLDKFQVAM VPGDAFGDDSCIRISYATSLDVLQAAVEKIRKALEPL Description Functional site 1) chain A residue 167 type sequence G description binding site for residue PLP A 701 source : AC1 2) chain A residue 168 type sequence A description binding site for residue PLP A 701 source : AC1 3) chain A residue 169 type sequence K description binding site for residue PLP A 701 source : AC1 4) chain A residue 193 type sequence W description binding site for residue PLP A 701 source : AC1 5) chain A residue 243 type sequence N description binding site for residue PLP A 701 source : AC1 6) chain A residue 272 type sequence D description binding site for residue PLP A 701 source : AC1 7) chain A residue 274 type sequence I description binding site for residue PLP A 701 source : AC1 8) chain A residue 275 type sequence Y description binding site for residue PLP A 701 source : AC1 9) chain A residue 305 type sequence S description binding site for residue PLP A 701 source : AC1 10) chain A residue 306 type sequence K description binding site for residue PLP A 701 source : AC1 11) chain A residue 314 type sequence R description binding site for residue PLP A 701 source : AC1 12) chain B residue 132 type sequence Y description binding site for residue PLP A 701 source : AC1 13) chain A residue 132 type sequence Y description binding site for residue PLP B 701 source : AC2 14) chain B residue 167 type sequence G description binding site for residue PLP B 701 source : AC2 15) chain B residue 168 type sequence A description binding site for residue PLP B 701 source : AC2 16) chain B residue 169 type sequence K description binding site for residue PLP B 701 source : AC2 17) chain B residue 193 type sequence W description binding site for residue PLP B 701 source : AC2 18) chain B residue 239 type sequence C description binding site for residue PLP B 701 source : AC2 19) chain B residue 243 type sequence N description binding site for residue PLP B 701 source : AC2 20) chain B residue 272 type sequence D description binding site for residue PLP B 701 source : AC2 21) chain B residue 274 type sequence I description binding site for residue PLP B 701 source : AC2 22) chain B residue 275 type sequence Y description binding site for residue PLP B 701 source : AC2 23) chain B residue 305 type sequence S description binding site for residue PLP B 701 source : AC2 24) chain B residue 306 type sequence K description binding site for residue PLP B 701 source : AC2 25) chain B residue 314 type sequence R description binding site for residue PLP B 701 source : AC2 26) chain C residue 167 type sequence G description binding site for residue PLP C 701 source : AC3 27) chain C residue 168 type sequence A description binding site for residue PLP C 701 source : AC3 28) chain C residue 169 type sequence K description binding site for residue PLP C 701 source : AC3 29) chain C residue 193 type sequence W description binding site for residue PLP C 701 source : AC3 30) chain C residue 243 type sequence N description binding site for residue PLP C 701 source : AC3 31) chain C residue 272 type sequence D description binding site for residue PLP C 701 source : AC3 32) chain C residue 274 type sequence I description binding site for residue PLP C 701 source : AC3 33) chain C residue 275 type sequence Y description binding site for residue PLP C 701 source : AC3 34) chain C residue 305 type sequence S description binding site for residue PLP C 701 source : AC3 35) chain C residue 306 type sequence K description binding site for residue PLP C 701 source : AC3 36) chain C residue 314 type sequence R description binding site for residue PLP C 701 source : AC3 37) chain D residue 132 type sequence Y description binding site for residue PLP C 701 source : AC3 38) chain C residue 132 type sequence Y description binding site for residue PLP D 701 source : AC4 39) chain D residue 167 type sequence G description binding site for residue PLP D 701 source : AC4 40) chain D residue 168 type sequence A description binding site for residue PLP D 701 source : AC4 41) chain D residue 169 type sequence K description binding site for residue PLP D 701 source : AC4 42) chain D residue 193 type sequence W description binding site for residue PLP D 701 source : AC4 43) chain D residue 239 type sequence C description binding site for residue PLP D 701 source : AC4 44) chain D residue 243 type sequence N description binding site for residue PLP D 701 source : AC4 45) chain D residue 272 type sequence D description binding site for residue PLP D 701 source : AC4 46) chain D residue 274 type sequence I description binding site for residue PLP D 701 source : AC4 47) chain D residue 275 type sequence Y description binding site for residue PLP D 701 source : AC4 48) chain D residue 305 type sequence S description binding site for residue PLP D 701 source : AC4 49) chain D residue 306 type sequence K description binding site for residue PLP D 701 source : AC4 50) chain D residue 314 type sequence R description binding site for residue PLP D 701 source : AC4 51) chain E residue 167 type sequence G description binding site for residue PLP E 701 source : AC5 52) chain E residue 168 type sequence A description binding site for residue PLP E 701 source : AC5 53) chain E residue 169 type sequence K description binding site for residue PLP E 701 source : AC5 54) chain E residue 193 type sequence W description binding site for residue PLP E 701 source : AC5 55) chain E residue 243 type sequence N description binding site for residue PLP E 701 source : AC5 56) chain E residue 272 type sequence D description binding site for residue PLP E 701 source : AC5 57) chain E residue 275 type sequence Y description binding site for residue PLP E 701 source : AC5 58) chain E residue 305 type sequence S description binding site for residue PLP E 701 source : AC5 59) chain E residue 306 type sequence K description binding site for residue PLP E 701 source : AC5 60) chain E residue 314 type sequence R description binding site for residue PLP E 701 source : AC5 61) chain F residue 132 type sequence Y description binding site for residue PLP E 701 source : AC5 62) chain E residue 132 type sequence Y description binding site for residue PLP F 701 source : AC6 63) chain F residue 167 type sequence G description binding site for residue PLP F 701 source : AC6 64) chain F residue 168 type sequence A description binding site for residue PLP F 701 source : AC6 65) chain F residue 169 type sequence K description binding site for residue PLP F 701 source : AC6 66) chain F residue 193 type sequence W description binding site for residue PLP F 701 source : AC6 67) chain F residue 272 type sequence D description binding site for residue PLP F 701 source : AC6 68) chain F residue 274 type sequence I description binding site for residue PLP F 701 source : AC6 69) chain F residue 275 type sequence Y description binding site for residue PLP F 701 source : AC6 70) chain F residue 305 type sequence S description binding site for residue PLP F 701 source : AC6 71) chain F residue 306 type sequence K description binding site for residue PLP F 701 source : AC6 72) chain A residue 107 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 73) chain C residue 193 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 74) chain C residue 243 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 75) chain C residue 445 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 76) chain D residue 107 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 77) chain D residue 193 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 78) chain D residue 243 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 79) chain D residue 445 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 80) chain E residue 107 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 81) chain E residue 193 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 82) chain E residue 243 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 83) chain A residue 193 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 84) chain E residue 445 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 85) chain F residue 107 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 86) chain F residue 193 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 87) chain F residue 243 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 88) chain F residue 445 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 89) chain A residue 243 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 90) chain A residue 445 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 91) chain B residue 107 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 92) chain B residue 193 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 93) chain B residue 243 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 94) chain B residue 445 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 95) chain C residue 107 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 96) chain A residue 306 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 97) chain B residue 306 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 98) chain C residue 306 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 99) chain D residue 306 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 100) chain E residue 306 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 101) chain F residue 306 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 102) chain A residue 303-316 type prosite sequence GFSKAFAMTGWRLG description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GFSKafAMtGWRLG source prosite : PS00105

Display surface Download Links