eF-site ID 5bj3-B PDB Code 5bj3 Chain B 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 B:  MRGLSRRVQAMKPLVALTAGEPDFDTPEHVKEAARRALAQ GKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVG GSQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVV VEVETLPEEGFVPDPERVRRAITPRTKALVVNSPNNPTGA VYPKEVLEALARLAVEHDFYLVSDEIYEHLLYEGEHFSPG RVAPEHTLTVNGAAKAFAMTGWRIGYACGPKEVIKAMASV SRQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRR RDLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAE RLLEAGVAVVPGTDFAAFGHVRLSYATSEENLRKALERFA RVL Description Functional site 1) chain B residue 64 type sequence Y description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 2) chain B residue 99 type sequence G description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 3) chain B residue 100 type sequence G description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 4) chain B residue 101 type sequence S description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 5) chain B residue 125 type sequence W description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 6) chain B residue 171 type sequence N description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 7) chain B residue 175 type sequence N description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 8) chain B residue 203 type sequence D description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 9) chain B residue 205 type sequence I description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 10) chain B residue 206 type sequence Y description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 11) chain B residue 233 type sequence A description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 12) chain B residue 234 type sequence K description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 13) chain B residue 242 type sequence R description BINDING SITE FOR RESIDUE PLP B 413 source : AC2 14) chain B residue 39 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 12 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 16) chain B 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 B residue 125 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 18) chain B residue 175 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 19) chain B residue 361 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2

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