eF-site ID 1gc3-D PDB Code 1gc3 Chain D click to enlarge Title THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH TRYPTOPHAN Classification TRANSFERASE Compound ASPARTATE AMINOTRANSFERASE Source (AAT_THETH) Sequence D:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL Description Functional site 1) chain D residue 1564 type sequence Y description BINDING SITE FOR RESIDUE TRP C 1414 source : AC3 2) chain D residue 1516 type sequence V description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 3) chain D residue 1520 type sequence N description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 4) chain D residue 1537 type sequence T description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 5) chain D residue 1539 type sequence G description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 6) chain D residue 1675 type sequence N description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 7) chain D residue 1734 type sequence K description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 8) chain D residue 1822 type sequence Y description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 9) chain D residue 1861 type sequence R description BINDING SITE FOR RESIDUE TRP D 1914 source : AC4 10) chain D residue 1564 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1413 source : BC2 11) chain D residue 1600 type sequence G description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 12) chain D residue 1601 type sequence S description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 13) chain D residue 1671 type sequence N description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 14) chain D residue 1675 type sequence N description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 15) chain D residue 1703 type sequence D description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 16) chain D residue 1706 type sequence Y description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 17) chain D residue 1734 type sequence K description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 18) chain D residue 1742 type sequence R description BINDING SITE FOR RESIDUE PLP D 1913 source : BC3 19) chain D residue 1539 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 20) chain D residue 1512 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 21) 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 22) chain D residue 1625 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 23) chain D residue 1675 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 24) chain D residue 1861 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2

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