eF-site ID 1asz-ABRS PDB Code 1asz Chain A, B, R, S click to enlarge Title THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION Classification COMPLEX (AMINOACYL-TRNA SYNTHASE/TRNA) Compound T-RNA (75-MER) Source (1ASZ) 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 R:  UCCGUGAUAGUUXAAXGGXCAGAAUGGGCGCXUGUCXCGU GCCAGAUXGGGGXXCAAUUCCCCGUCGCGGAGCCA S:  UCCGUGAUAGUUXAAXGGXCAGAAUGGGCGCXUGUCXCGU GCCAGAUXGGGGXXCAAUUCCCCGUCGCGGAGCCA Description Functional site 1) chain A residue 325 type sequence R description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 2) chain A residue 334 type sequence H description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 3) chain A residue 335 type sequence M description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 4) chain A residue 338 type sequence F description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 5) chain A residue 478 type sequence E description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 6) chain A residue 479 type sequence I description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 7) chain A residue 480 type sequence L description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 8) chain A residue 526 type sequence G description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 9) chain A residue 531 type sequence R description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 10) chain R residue 675 type sequence C description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 11) chain R residue 676 type sequence A description BINDING SITE FOR RESIDUE ATP A 701 source : AC1 12) chain B residue 325 type sequence R description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 13) chain B residue 335 type sequence M description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 14) chain B residue 338 type sequence F description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 15) chain B residue 478 type sequence E description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 16) chain B residue 479 type sequence I description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 17) chain B residue 480 type sequence L description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 18) chain B residue 481 type sequence S description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 19) chain B residue 527 type sequence I description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 20) chain B residue 531 type sequence R description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 21) chain S residue 675 type sequence C description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 22) chain S residue 676 type sequence A description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 23) chain A residue 326 type catalytic sequence A description 404 source MCSA : MCSA1 24) chain A residue 328 type catalytic sequence N description 404 source MCSA : MCSA1 25) chain A residue 334 type catalytic sequence H description 404 source MCSA : MCSA1 26) chain A residue 335 type catalytic sequence M description 404 source MCSA : MCSA1 27) chain A residue 479 type catalytic sequence I description 404 source MCSA : MCSA1 28) chain A residue 482 type catalytic sequence G description 404 source MCSA : MCSA1 29) chain A residue 532 type catalytic sequence V description 404 source MCSA : MCSA1 30) chain B residue 326 type catalytic sequence A description 404 source MCSA : MCSA2 31) chain B residue 328 type catalytic sequence N description 404 source MCSA : MCSA2 32) chain B residue 334 type catalytic sequence H description 404 source MCSA : MCSA2 33) chain B residue 335 type catalytic sequence M description 404 source MCSA : MCSA2 34) chain B residue 479 type catalytic sequence I description 404 source MCSA : MCSA2 35) chain B residue 482 type catalytic sequence G description 404 source MCSA : MCSA2 36) chain B residue 532 type catalytic sequence V description 404 source MCSA : MCSA2 37) chain A residue 282 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 326 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 334 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 479 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 482 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 486 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 334 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 479 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 482 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 486 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 529 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 529 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 282 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 50) chain B residue 326 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 51) 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 52) 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 53) 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 54) 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 55) chain A residue 547 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI4 56) 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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