Structure of PDB 1kog Chain C Binding Site BS02

Receptor Information
>1kog Chain C (length=401) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQ
EVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIF
NQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEE
QIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADL
AVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPS
RLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQ
VVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVP
YMLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLE
E
Ligand information
>1kog Chain L (length=37) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ggcguaugugaucuuucgugugggucaccacugcgcc
<<<<<..<<<<<<<.......>>>>>>>....>>>>>
Receptor-Ligand Complex Structure
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PDB1kog Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.
Resolution3.5 Å
Binding residue
(original residue number in PDB)		G344 L345 S347 Y348 R349 V498 G499 E500 N502
Binding residue
(residue number reindexed from 1)		G103 L104 S106 Y107 R108 V257 G258 E259 N261
Binding affinityPDBbind-CN: Kd=0.01uM
Enzymatic activity
Catalytic site (original residue number in PDB) Q381 D383 K465
Catalytic site (residue number reindexed from 1) Q140 D142 K224
Enzyme Commision number 6.1.1.3: threonine--tRNA ligase.
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:1kog, PDBe:1kog, PDBj:1kog
PDBsum1kog
PubMed11953757
UniProtP0A8M3|SYT_ECOLI Threonine--tRNA ligase (Gene Name=thrS)

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