Structure of PDB 8i27 Chain A

Receptor sequence
>8i27A (length=323) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQD
AQKLRKATLDTLALYLACGIDPEKSTIFVQSHVPEHAQLGWALNCYTYFG
ELSRMTENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQ
RFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLED
PKSVVKKIKRAVTDSDEPPVVRYDVQNKAGVSNLLDILSAVTGQSIPELE
KQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEK
ASAHASRTLKAVYEAIGFVAKRH
3D structure
PDB8i27 An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening.
ChainA
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.2: tryptophan--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 O8C A A89 G92 W93 N96 D127 V130 A87 G90 W91 N94 D115 V118
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004830 tryptophan-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006436 tryptophanyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8i27, PDBe:8i27, PDBj:8i27
PDBsum8i27
PubMed37070195
UniProtP00954|SYW_ECOLI Tryptophan--tRNA ligase (Gene Name=trpS)

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