eF-site ID 1asy-AB PDB Code 1asy Chain A, B click to enlarge Title CLASS II AMINOACYL TRANSFER RNA SYNTHETASES: CRYSTAL STRUCTURE OF YEAST ASPARTYL-TRNA SYNTHETASE COMPLEXED WITH TRNA ASP Classification COMPLEX (AMINOACYL-TRNA SYNTHASE/TRNA) Compound T-RNA (75-MER) Source (1ASY) Sequence A:  EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDK EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEG TISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVN LDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAF EEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVE EFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPG LKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL FPRDPKRLRP B:  EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDK EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEG TISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVN LDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAF EEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVE EFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPG LKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL FPRDPKRLRP Description Functional site 1) chain A residue 326 type catalytic sequence A description 404 source MCSA : MCSA1 2) chain A residue 328 type catalytic sequence N description 404 source MCSA : MCSA1 3) chain A residue 334 type catalytic sequence H description 404 source MCSA : MCSA1 4) chain A residue 335 type catalytic sequence M description 404 source MCSA : MCSA1 5) chain A residue 479 type catalytic sequence I description 404 source MCSA : MCSA1 6) chain A residue 482 type catalytic sequence G description 404 source MCSA : MCSA1 7) chain A residue 532 type catalytic sequence V description 404 source MCSA : MCSA1 8) chain B residue 326 type catalytic sequence A description 404 source MCSA : MCSA2 9) chain B residue 328 type catalytic sequence N description 404 source MCSA : MCSA2 10) chain B residue 334 type catalytic sequence H description 404 source MCSA : MCSA2 11) chain B residue 335 type catalytic sequence M description 404 source MCSA : MCSA2 12) chain B residue 479 type catalytic sequence I description 404 source MCSA : MCSA2 13) chain B residue 482 type catalytic sequence G description 404 source MCSA : MCSA2 14) chain B residue 532 type catalytic sequence V description 404 source MCSA : MCSA2 15) chain A residue 282 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 334 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 479 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 482 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 486 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 529 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 326 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 334 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 479 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 482 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 486 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 529 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 282 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 326 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 302 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 302 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 503 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI3 32) chain B residue 503 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 547 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI4 34) chain B residue 547 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI4

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