Structure of PDB 8i2j Chain A

Receptor sequence
>8i2jA (length=321) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KPIVFSGAQPSGELTIGNYMGALRQWVNMQDDYHCIYCIVDQHAITVRQD
AQKLRKATLDTLALYLACGIDPEKSTIFVQSHVPEHAQLGWALNCYTYFG
ELSRMTENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQ
RFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKDDNRNNVIGLLEDP
KSVVKKIKRAVTDSDEPPVVRYDVQNKAGVSNLLDILSAVTGQSIPELEK
QFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKA
SAHASRTLKAVYEAIGFVAKR
3D structure
PDB8i2j An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening.
ChainA
Resolution2.65 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 O9F A G92 W93 N96 L131 G90 W91 N94 L119
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8i2j, PDBe:8i2j, PDBj:8i2j
PDBsum8i2j
PubMed37070195
UniProtP00954|SYW_ECOLI Tryptophan--tRNA ligase (Gene Name=trpS)

[Back to BioLiP]