Structure of PDB 1asy Chain B Binding Site BS01

Receptor Information
>1asy Chain B (length=490) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHN
TRQQGATLAFLTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVL
VRGIVKKVDEPIKSATVQNLEIHITKIYTISETPEALPILLEDASRSEAE
AEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKF
TEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERV
YEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFS
ELPKRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIG
DFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYS
NSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKDYCDGFSY
GCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP
Ligand information
>1asy Chain S (length=75) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
uccgugauaguuuaauggucagaaugggcgcuugucgcgugccagaucgg
gguucaauuccccgucgcggagcca
<<<<<<<..<<<<........>>>>.<<<<<.......>>>>>....<<<
<<.......>>>>>>>>>>>>....
Receptor-Ligand Complex Structure
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PDB1asy Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp).
Resolution2.9 Å
Binding residue
(original residue number in PDB)
R119 Q120 Q121 G122 L125 F127 Q138 L140 K142 I179 K180 S181 E188 L207 L223 V225 N227 D229 S280 E281 G283 S284 S301 Q303 F304 E327 N328 S329 N330 H334 S423 T424 E425 K428 P454 Y456
Binding residue
(residue number reindexed from 1)
R52 Q53 Q54 G55 L58 F60 Q71 L73 K75 I112 K113 S114 E121 L140 L156 V158 N160 D162 S213 E214 G216 S217 S234 Q236 F237 E260 N261 S262 N263 H267 S356 T357 E358 K361 P387 Y389
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.
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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