Structure of PDB 1asz Chain A Binding Site BS01

Receptor Information
>1asz Chain A (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
>1asz Chain R (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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PDB1asz The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction.
Resolution3.0 Å
Binding residue
(original residue number in PDB)
R119 Q120 Q121 T124 L125 F127 Q138 L140 E177 I179 K180 E202 P205 L207 A221 L223 P224 V225 N227 T230 S280 E281 G282 G283 S284 Q300 F304 E327 N328 S329 N330 H334 S423 T424 F455 K553
Binding residue
(residue number reindexed from 1)
R52 Q53 Q54 T57 L58 F60 Q71 L73 E110 I112 K113 E135 P138 L140 A154 L156 P157 V158 N160 T163 S213 E214 G215 G216 S217 Q233 F237 E260 N261 S262 N263 H267 S356 T357 F388 K486
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:1asz, PDBe:1asz, PDBj:1asz
PDBsum1asz
PubMed8313877
UniProtP04802|SYDC_YEAST Aspartate--tRNA ligase, cytoplasmic (Gene Name=DPS1)

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