Structure of PDB 8i2a Chain B

Receptor sequence
>8i2aB (length=329) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TKPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQ
DAQKLRKATLDTLALYLACGIDPEKSTIFVQSHVPEHAQLGWALNCYTYF
GELSRMTQFKDKSENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLE
LSRDIAQRFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNN
VIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNKAGVSNLLDILSAVTG
QSIPELEKQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQV
MKDGAEKASAHASRTLKAVYEAIGFVAKR
3D structure
PDB8i2a An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening.
ChainB
Resolution2.35 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 TYM B S8 G9 Q11 G19 N20 G23 V42 Y128 M132 I136 V146 G147 D149 Q150 A184 R185 V186 K195 K198 S7 G8 Q10 G18 N19 G22 V41 Y123 M127 I131 V141 G142 D144 Q145 A179 R180 V181 K190 K193
BS02 5OB B G92 W93 N96 D127 G91 W92 N95 D122
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:8i2a, PDBe:8i2a, PDBj:8i2a
PDBsum8i2a
PubMed37070195
UniProtP00954|SYW_ECOLI Tryptophan--tRNA ligase (Gene Name=trpS)

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