Structure of PDB 8i27 Chain B

Receptor sequence
>8i27B (length=333) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQ
DAQKLRKATLDTLALYLACGIDPEKSTIFVQSHVPEHAQLGWALNCYTYF
GELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQK
QHLELSRDIAQRFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDD
NRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNKAGVSNLLDILS
AVTGQSIPELEKQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAF
LQQVMKDGAEKASAHASRTLKAVYEAIGFVAKR
3D structure
PDB8i27 An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening.
ChainB
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 B A89 G92 W93 A88 G91 W92
BS02 TYM B S8 G9 A10 Q11 G19 N20 G23 A24 V42 H45 Y128 M132 I136 V144 V146 G147 D149 Q150 A184 R185 V186 K195 K198 S7 G8 A9 Q10 G18 N19 G22 A23 V41 H44 Y127 M131 I135 V143 V145 G146 D148 Q149 A183 R184 V185 K194 K197
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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