Structure of PDB 1b8a Chain A

Receptor sequence
>1b8aA (length=438) Species: 69014 (Thermococcus kodakarensis KOD1) [Search protein sequence]
MYRTHYSSEITEELNGQKVKVAGWVWEVKDLGGIKFLWIRDRDGIVQITA
PKKKVDPELFKLIPKLRSEDVVAVEGVVNFTPKAKLGFEILPEKIVVLNR
AETPLPLDPTGKVKAELDTRLNNRFMDLRRPEVMAIFKIRSSVFKAVRDF
FHENGFIEIHTPKIIATATEGGTELFPMKYFEEDAFLAESPQLYKEIMMA
SGLDRVYEIAPIFRAEEHNTTRHLNEAWSIDSEMAFIEDEEEVMSFLERL
VAHAINYVREHNAKELDILNFELEEPKLPFPRVSYDKALEILGDLGKEIP
WGEDIDTEGERLLGKYMMENENAPLYFLYQYPSEAKPFYIMKYDNKPEIC
RAFDLEYRGVEISSGGQREHRHDILVEQIKEKGLNPESFEFYLKAFRYGM
PPHGGFGLGAERLIKQMLDLPNIREVILFPRDRRRLTP
3D structure
PDB1b8a Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.12: aspartate--tRNA ligase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN A E361 S364 E361 S364
BS02 ATP A R214 E216 H223 L224 E361 I362 S363 S364 G409 R412 R214 E216 H223 L224 E361 I362 S363 S364 G409 R412
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0003676 nucleic acid binding
GO:0003723 RNA binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004815 aspartate-tRNA ligase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006422 aspartyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0017101 aminoacyl-tRNA synthetase multienzyme complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1b8a, PDBe:1b8a, PDBj:1b8a
PDBsum1b8a
PubMed9724658
UniProtQ52428|SYD_THEKO Aspartate--tRNA(Asp) ligase (Gene Name=aspS)

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