Structure of PDB 3ko4 Chain C

Receptor sequence
>3ko4C (length=151) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
MRVVIQRVKGAILSVRKELEIISEIKNGLICFLGIHKNDTWEDALYIIRK
CLNLRLWNNNKTWDKNVKDLNYELLIVSQFTLFGNTKKGNKPDFHLAKEP
NEALIFYNKIIDEFKKQYNDDKIKIGKFGNYMNIDVTNDGPVTIYIDTHD
I
3D structure
PDB3ko4 Ligand-bound Structures Provide Atomic Snapshots for the Catalytic Mechanism of D-Amino Acid Deacylase
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q88 F89 T90
Catalytic site (residue number reindexed from 1) Q79 F80 T81
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 ADP C T71 W72 T62 W63
BS02 ADP C F89 F103 A106 P109 F80 F94 A97 P100
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0002161 aminoacyl-tRNA editing activity
GO:0016787 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: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:3ko4, PDBe:3ko4, PDBj:3ko4
PDBsum3ko4
PubMed20007323
UniProtQ8IIS0|DTD_PLAF7 D-aminoacyl-tRNA deacylase (Gene Name=DTD)

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