Structure of PDB 1jke Chain A

Receptor sequence
>1jkeA (length=145) Species: 562 (Escherichia coli) [Search protein sequence]
MIALIQRVTRASVTVEGEVTGEIGAGLLVLLGVEKDDDEQKANRLCERVL
GYRIFSDAEGKMNLNVQQAGGSVLVVSQFTLAADTERGMRPSFSKGASPD
RAEALYDYFVERCRQQEMNTQTGRFAADMQVSLVNDGPVTFWLQV
3D structure
PDB1jke Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases.
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q78 F79 T80
Catalytic site (residue number reindexed from 1) Q78 F79 T80
Enzyme Commision number 3.1.1.96: D-aminoacyl-tRNA deacylase.
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 ZN A E103 D107 E103 D107
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0002161 aminoacyl-tRNA editing activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0042803 protein homodimerization activity
GO:0043908 Ser(Gly)-tRNA(Ala) hydrolase activity
GO:0051499 D-aminoacyl-tRNA deacylase activity
GO:0051500 D-tyrosyl-tRNA(Tyr) deacylase activity
GO:0106026 Gly-tRNA(Ala) hydrolase activity
Biological Process
GO:0006399 tRNA metabolic process
GO:0009408 response to heat
GO:0019478 D-amino acid catabolic process
GO:0106074 aminoacyl-tRNA metabolism involved in translational fidelity
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:1jke, PDBe:1jke, PDBj:1jke
PDBsum1jke
PubMed11568181
UniProtP0A6M4|DTD_ECOLI D-aminoacyl-tRNA deacylase (Gene Name=dtd)

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