Structure of PDB 1asy Chain B

Receptor sequence
>1asyB (length=490) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHN
TRQQGATLAFLTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVL
VRGIVKKVDEPIKSATVQNLEIHITKIYTISETPEALPILLEDASRSEAE
AEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF
TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERV
YEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFS
ELPKRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIG
DFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS
NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKDYCDGFSY
GCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP
3D structure
PDB1asy Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp).
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R325 E327 R333 H334 E478 S481 R531
Catalytic site (residue number reindexed from 1) R258 E260 R266 H267 E411 S414 R464
Enzyme Commision number 6.1.1.12: aspartate--tRNA ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004815 aspartate-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006422 aspartyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1asy, PDBe:1asy, PDBj:1asy
PDBsum1asy
PubMed2047877
UniProtP04802|SYDC_YEAST Aspartate--tRNA ligase, cytoplasmic (Gene Name=DPS1)

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