eF-site ID 1gc3-EFGH PDB Code 1gc3 Chain E, F, G, H click to enlarge Title THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH TRYPTOPHAN Classification TRANSFERASE Compound ASPARTATE AMINOTRANSFERASE Source (AAT_THETH) Sequence E:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL F:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL G:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL H:  MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGE PDFDTPEHVKEAARRALAQGKTKYAPPAGIPELREALAEK FRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVIV LSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRA ITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTG WRIGYACGPKEVIKAMASVSRQSTTSPDTIAQWATLEALT NQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSGA FYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHV RLSYATSEENLRKALERFARVL Description Functional site 1) chain E residue 2039 type sequence G description BINDING SITE FOR RESIDUE TRP E 2414 source : AC5 2) chain E residue 2322 type sequence Y description BINDING SITE FOR RESIDUE TRP E 2414 source : AC5 3) chain E residue 2361 type sequence R description BINDING SITE FOR RESIDUE TRP E 2414 source : AC5 4) chain E residue 2064 type sequence Y description BINDING SITE FOR RESIDUE TRP E 2914 source : AC6 5) chain F residue 2516 type sequence V description BINDING SITE FOR RESIDUE TRP E 2914 source : AC6 6) chain F residue 2539 type sequence G description BINDING SITE FOR RESIDUE TRP E 2914 source : AC6 7) chain F residue 2734 type sequence K description BINDING SITE FOR RESIDUE TRP E 2914 source : AC6 8) chain F residue 2822 type sequence Y description BINDING SITE FOR RESIDUE TRP E 2914 source : AC6 9) chain F residue 2861 type sequence R description BINDING SITE FOR RESIDUE TRP E 2914 source : AC6 10) chain G residue 3016 type sequence V description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 11) chain G residue 3020 type sequence N description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 12) chain G residue 3037 type sequence T description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 13) chain G residue 3039 type sequence G description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 14) chain G residue 3040 type sequence E description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 15) chain G residue 3125 type sequence W description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 16) chain G residue 3175 type sequence N description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 17) chain G residue 3361 type sequence R description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 18) chain H residue 3564 type sequence Y description BINDING SITE FOR RESIDUE TRP G 3414 source : AC7 19) chain H residue 3516 type sequence V description BINDING SITE FOR RESIDUE TRP H 3914 source : AC8 20) chain H residue 3520 type sequence N description BINDING SITE FOR RESIDUE TRP H 3914 source : AC8 21) chain H residue 3537 type sequence T description BINDING SITE FOR RESIDUE TRP H 3914 source : AC8 22) chain H residue 3539 type sequence G description BINDING SITE FOR RESIDUE TRP H 3914 source : AC8 23) chain H residue 3675 type sequence N description BINDING SITE FOR RESIDUE TRP H 3914 source : AC8 24) chain H residue 3822 type sequence Y description BINDING SITE FOR RESIDUE TRP H 3914 source : AC8 25) chain H residue 3861 type sequence R description BINDING SITE FOR RESIDUE TRP H 3914 source : AC8 26) chain E residue 2099 type sequence G description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 27) chain E residue 2100 type sequence G description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 28) chain E residue 2101 type sequence S description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 29) chain E residue 2125 type sequence W description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 30) chain E residue 2175 type sequence N description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 31) chain E residue 2203 type sequence D description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 32) chain E residue 2206 type sequence Y description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 33) chain E residue 2233 type sequence A description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 34) chain E residue 2242 type sequence R description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 35) chain E residue 2322 type sequence Y description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 36) chain F residue 2564 type sequence Y description BINDING SITE FOR RESIDUE PLP E 2413 source : BC4 37) chain E residue 2064 type sequence Y description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 38) chain F residue 2600 type sequence G description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 39) chain F residue 2601 type sequence S description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 40) chain F residue 2625 type sequence W description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 41) chain F residue 2675 type sequence N description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 42) chain F residue 2703 type sequence D description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 43) chain F residue 2706 type sequence Y description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 44) chain F residue 2734 type sequence K description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 45) chain F residue 2742 type sequence R description BINDING SITE FOR RESIDUE PLP F 2913 source : BC5 46) chain G residue 3100 type sequence G description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 47) chain G residue 3101 type sequence S description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 48) chain G residue 3125 type sequence W description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 49) chain G residue 3171 type sequence N description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 50) chain G residue 3175 type sequence N description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 51) chain G residue 3203 type sequence D description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 52) chain G residue 3206 type sequence Y description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 53) chain G residue 3242 type sequence R description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 54) chain H residue 3564 type sequence Y description BINDING SITE FOR RESIDUE PLP G 3413 source : BC6 55) chain G residue 3064 type sequence Y description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 56) chain H residue 3599 type sequence G description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 57) chain H residue 3600 type sequence G description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 58) chain H residue 3601 type sequence S description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 59) chain H residue 3625 type sequence W description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 60) chain H residue 3675 type sequence N description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 61) chain H residue 3703 type sequence D description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 62) chain H residue 3706 type sequence Y description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 63) chain H residue 3734 type sequence K description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 64) chain H residue 3742 type sequence R description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 65) chain H residue 3822 type sequence Y description BINDING SITE FOR RESIDUE PLP H 3913 source : BC7 66) chain E residue 2039 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 67) chain F residue 2539 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 68) chain G residue 3039 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 69) chain H residue 3539 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00509 source Swiss-Prot : SWS_FT_FI1 70) chain E residue 2012 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 71) chain F residue 2512 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 72) chain G residue 3012 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 73) chain H residue 3512 type SITE sequence K description Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 source Swiss-Prot : SWS_FT_FI3 74) chain E residue 2234 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 75) chain F residue 2734 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 76) chain G residue 3234 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 77) chain H residue 3734 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 78) chain E residue 2125 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 79) chain E residue 2175 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 80) chain E residue 2361 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 81) chain F residue 2625 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 82) chain F residue 2675 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 83) chain F residue 2861 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 84) chain G residue 3125 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 85) chain G residue 3175 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 86) chain G residue 3361 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 87) chain H residue 3625 type BINDING sequence W description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 88) chain H residue 3675 type BINDING sequence N description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2 89) chain H residue 3861 type BINDING sequence R description BINDING => ECO:0007744|PDB:1GCK source Swiss-Prot : SWS_FT_FI2

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