eF-site ID 5bj3-D PDB Code 5bj3 Chain D click to enlarge Title THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 1 Classification TRANSFERASE Compound PROTEIN (ASPARTATE AMINOTRANSFERASE) Source Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (AAT_THET8) Sequence D:  MRGLSRRVQAMKPLVALTAGEPDFDTPEHVKEAARRALAQ GKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVG GSQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVV VEVETLPEEGFVPDPERVRRAITPRTKALVVNSPNNPTGA VYPKEVLEALARLAVEHDFYLVSDEIYEHLLYEGEHFSPG RVAPEHTLTVNGAAKAFAMTGWRIGYACGPKEVIKAMASV SRQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRR RDLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAE RLLEAGVAVVPGTDFAAFGHVRLSYATSEENLRKALERFA RVL Description Functional site 1) chain D residue 64 type sequence Y description BINDING SITE FOR RESIDUE PLP C 413 source : AC3 2) chain D residue 99 type sequence G description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 3) chain D residue 100 type sequence G description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 4) chain D residue 101 type sequence S description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 5) chain D residue 125 type sequence W description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 6) chain D residue 171 type sequence N description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 7) chain D residue 175 type sequence N description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 8) chain D residue 203 type sequence D description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 9) chain D residue 205 type sequence I description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 10) chain D residue 206 type sequence Y description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 11) chain D residue 233 type sequence A description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 12) chain D residue 234 type sequence K description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 13) chain D residue 242 type sequence R description BINDING SITE FOR RESIDUE PLP D 413 source : AC4 14) chain D residue 39 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 15) chain D residue 12 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 16) chain D 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 17) chain D residue 125 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 18) chain D residue 175 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 19) chain D residue 361 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2

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