Structure of PDB 8ou8 Chain D

Receptor sequence
>8ou8D (length=399) Species: 585034 (Escherichia coli IAI1) [Search protein sequence]
DHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQE
VKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIFN
QGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEEQ
IRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADLA
VALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPSR
LSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQV
VIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVPY
MLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLE
3D structure
PDB8ou8 Synthesis and evaluation of an agrocin 84 toxic moiety (TM84) analogue as a malarial threonyl tRNA synthetase inhibitor.
ChainD
Resolution2.05 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.3: threonine--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 W0U D M91 R122 E124 M133 V135 F138 Q140 D142 H144 Y221 K224 Q238 T241 Q243 H270 S276 R279 M90 R121 E123 M132 V134 F137 Q139 D141 H143 Y220 K223 Q237 T240 Q242 H269 S275 R278
BS02 ZN D C93 H144 H270 C92 H143 H269
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004829 threonine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006435 threonyl-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:8ou8, PDBe:8ou8, PDBj:8ou8
PDBsum8ou8
PubMed37335076
UniProtP0A8M3|SYT_ECOLI Threonine--tRNA ligase (Gene Name=thrS)

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