Structure of PDB 1kog Chain E Binding Site BS02

Receptor Information

>1kog Chain E (length=401) Species: 562 (Escherichia coli)

RDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQ
EVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIF
NQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEE
QIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADL
AVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPS
RLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQ
VVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVP
YMLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLE
E

Ligand information

>1kog Chain N (length=37)

ggcguaugugaucuuucgugugggucaccacugcgcc

<<<<<..<<<<<<<.......>>>>>>>....>>>>>

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1kog Structural basis of translational control by Escherichia coli threonyl tRNA synthetase.
• Resolution: 3.5 Å
• Binding residue (original residue number in PDB): L345 S347 Y348 R349 V498 E500 N502
• Binding residue (residue number reindexed from 1): L104 S106 Y107 R108 V257 E259 N261
• Binding affinity: PDBbind-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

External links

• PDB: RCSB:1kog, PDBe:1kog, PDBj:1kog
• PDBsum: 1kog
• PubMed: 11953757
• UniProt: P0A8M3|SYT_ECOLI Threonine--tRNA ligase (Gene Name=thrS)