eF-site ID 1gc3-ABCD PDB Code 1gc3 Chain A, B, C, D click to enlarge Title THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH TRYPTOPHAN Classification TRANSFERASE Compound ASPARTATE AMINOTRANSFERASE Source (AAT_THETH) Sequence A:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL B:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL C:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL D:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL Description Functional site 1) chain A residue 16 type sequence V description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 2) chain A residue 20 type sequence N description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 3) chain A residue 37 type sequence T description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 4) chain A residue 38 type sequence A description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 5) chain A residue 39 type sequence G description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 6) chain A residue 40 type sequence E description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 7) chain A residue 175 type sequence N description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 8) chain A residue 322 type sequence Y description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 9) chain A residue 361 type sequence R description BINDING SITE FOR RESIDUE TRP A 414 source : AC1 10) chain A residue 64 type sequence Y description BINDING SITE FOR RESIDUE TRP A 914 source : AC2 11) chain A residue 265 type sequence T description BINDING SITE FOR RESIDUE TRP A 914 source : AC2 12) chain B residue 516 type sequence V description BINDING SITE FOR RESIDUE TRP A 914 source : AC2 13) chain B residue 539 type sequence G description BINDING SITE FOR RESIDUE TRP A 914 source : AC2 14) chain B residue 675 type sequence N description BINDING SITE FOR RESIDUE TRP A 914 source : AC2 15) chain B residue 734 type sequence K description BINDING SITE FOR RESIDUE TRP A 914 source : AC2 16) chain B residue 822 type sequence Y description BINDING SITE FOR RESIDUE TRP A 914 source : AC2 17) chain B residue 861 type sequence R description BINDING SITE FOR RESIDUE TRP A 914 source : AC2 18) chain C residue 1016 type sequence V description BINDING SITE FOR RESIDUE TRP C 1414 source : AC3 19) chain C residue 1020 type sequence N description BINDING SITE FOR RESIDUE TRP C 1414 source : AC3 20) chain C residue 1039 type sequence G description BINDING SITE FOR RESIDUE TRP C 1414 source : AC3 21) chain C residue 1234 type sequence K description BINDING SITE FOR RESIDUE TRP C 1414 source : AC3 22) chain C residue 1322 type sequence Y description BINDING SITE FOR RESIDUE TRP C 1414 source : AC3 23) chain C residue 1361 type sequence R description BINDING SITE FOR RESIDUE TRP C 1414 source : AC3 24) chain D residue 1564 type sequence Y description BINDING SITE FOR RESIDUE TRP C 1414 source : AC3 25) chain C residue 1064 type sequence Y description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 26) chain D residue 1516 type sequence V description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 27) chain D residue 1520 type sequence N description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 28) chain D residue 1537 type sequence T description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 29) chain D residue 1539 type sequence G description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 30) chain D residue 1675 type sequence N description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 31) chain D residue 1734 type sequence K description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 32) chain D residue 1822 type sequence Y description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 33) chain D residue 1861 type sequence R description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 34) chain A residue 99 type sequence G description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 35) chain A residue 100 type sequence G description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 36) chain A residue 101 type sequence S description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 37) chain A residue 171 type sequence N description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 38) chain A residue 175 type sequence N description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 39) chain A residue 203 type sequence D description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 40) chain A residue 206 type sequence Y description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 41) chain A residue 234 type sequence K description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 42) chain A residue 242 type sequence R description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 43) chain A residue 322 type sequence Y description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 44) chain B residue 564 type sequence Y description BINDING SITE FOR RESIDUE PLP A 413 source : AC9 45) chain A residue 64 type sequence Y description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 46) chain B residue 600 type sequence G description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 47) chain B residue 601 type sequence S description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 48) chain B residue 625 type sequence W description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 49) chain B residue 671 type sequence N description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 50) chain B residue 675 type sequence N description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 51) chain B residue 703 type sequence D description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 52) chain B residue 706 type sequence Y description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 53) chain B residue 734 type sequence K description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 54) chain B residue 742 type sequence R description BINDING SITE FOR RESIDUE PLP B 913 source : BC1 55) chain C residue 1100 type sequence G description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 56) chain C residue 1101 type sequence S description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 57) chain C residue 1125 type sequence W description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 58) chain C residue 1175 type sequence N description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 59) chain C residue 1203 type sequence D description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 60) chain C residue 1206 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 61) chain C residue 1233 type sequence A description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 62) chain C residue 1234 type sequence K description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 63) chain C residue 1242 type sequence R description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 64) chain C residue 1322 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 65) chain D residue 1564 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 66) chain C residue 1064 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 67) chain D residue 1600 type sequence G description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 68) chain D residue 1601 type sequence S description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 69) chain D residue 1671 type sequence N description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 70) chain D residue 1675 type sequence N description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 71) chain D residue 1703 type sequence D description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 72) chain D residue 1706 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 73) chain D residue 1734 type sequence K description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 74) chain D residue 1742 type sequence R description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 75) chain A residue 39 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 539 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 77) chain C residue 1039 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 78) chain D residue 1539 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 79) chain A residue 12 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 80) chain B residue 512 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 81) chain C residue 1012 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 82) chain D residue 1512 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 83) chain A residue 234 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4 source Swiss-Prot : SWS_FT_FI4 84) chain B residue 734 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4 source Swiss-Prot : SWS_FT_FI4 85) chain C residue 1234 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4 source Swiss-Prot : SWS_FT_FI4 86) chain D residue 1734 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10029535, ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4 source Swiss-Prot : SWS_FT_FI4 87) chain A residue 125 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 88) chain D residue 1625 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 89) chain D residue 1675 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 90) chain D residue 1861 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 91) chain A residue 175 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 92) chain A residue 361 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 93) chain B residue 625 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 94) chain B residue 675 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 95) chain B residue 861 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 96) chain C residue 1125 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 97) chain C residue 1175 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 98) chain C residue 1361 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 99) chain A residue 231-244 type prosite sequence GAAKAFAMTGWRIG description AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GAAKafAMtGWRIG source prosite : PS00105

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