eF-site ID 1asz-B PDB Code 1asz Chain B 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 B:  EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDK EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEG TISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVN LDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAF EEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVE EFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPG LKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL FPRDPKRLRP Description Functional site 1) chain B residue 325 type sequence R description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 2) chain B residue 335 type sequence M description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 3) chain B residue 338 type sequence F description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 4) chain B residue 478 type sequence E description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 5) chain B residue 479 type sequence I description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 6) chain B residue 480 type sequence L description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 7) chain B residue 481 type sequence S description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 8) chain B residue 527 type sequence I description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 9) chain B residue 531 type sequence R description BINDING SITE FOR RESIDUE ATP B 701 source : AC2 10) chain B residue 326 type catalytic sequence A description 404 source MCSA : MCSA2 11) chain B residue 328 type catalytic sequence N description 404 source MCSA : MCSA2 12) chain B residue 334 type catalytic sequence H description 404 source MCSA : MCSA2 13) chain B residue 335 type catalytic sequence M description 404 source MCSA : MCSA2 14) chain B residue 479 type catalytic sequence I description 404 source MCSA : MCSA2 15) chain B residue 482 type catalytic sequence G description 404 source MCSA : MCSA2 16) chain B residue 532 type catalytic sequence V description 404 source MCSA : MCSA2 17) chain B residue 334 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 479 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 482 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 486 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 529 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 282 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 326 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) 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 25) 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 26) 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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