Structure of PDB 1jke Chain D Binding Site BS01
Receptor Information
>1jke Chain D (length=145) Species:
562
(Escherichia coli) [
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MIALIQRVTRASVTVEGEVTGEIGAGLLVLLGVEKDDDEQKANRLCERVL
GYRIFSDAEGKMNLNVQQAGGSVLVVSQFTLAADTERGMRPSFSKGASPD
RAEALYDYFVERCRQQEMNTQTGRFAADMQVSLVNDGPVTFWLQV
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1jke Chain D Residue 902 [
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Receptor-Ligand Complex Structure
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PDB
1jke
Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases.
Resolution
1.55 Å
Binding residue
(original residue number in PDB)
E103 D107
Binding residue
(residue number reindexed from 1)
E103 D107
Annotation score
1
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.
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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Biological Process
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Cellular Component
External links
PDB
RCSB:1jke
,
PDBe:1jke
,
PDBj:1jke
PDBsum
1jke
PubMed
11568181
UniProt
P0A6M4
|DTD_ECOLI D-aminoacyl-tRNA deacylase (Gene Name=dtd)
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