Structure of PDB 1jil Chain A

Receptor sequence
>1jilA (length=323) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
TNVLIEDLKWRGLIYQQTDEQGIEDLLNKEQVTLYCGADPTADSLHIGHL
LPFLTLRRFQEHGHRPIVLIGGGTGMIGDPSGKSEERVLQTEEQVDKNIE
GISKQMHNIFEFGTDHGAVLVNNRDWLGQISLISFLRDYGKHVGVNYMLG
KDSIQSRLEHGISYTEFTYTILQAIDFGHLNRELNCKIQVGGSDQWGNIT
SGIELMRRMYGQTDAYGLTIPLVTKSDGKKFGKSESGAVWLDAEKTSPYE
FYQFWINQSDEDVIKFLKYFTFLGKEEIDRLEQSKNEAPHLREAQKTLAE
EVTKFIHGEDALNDAIRISQALF
3D structure
PDB1jil Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T42 H47 H50 K84 R88 Q174 D195 K231 K234 S235
Catalytic site (residue number reindexed from 1) T41 H46 H49 K83 R87 Q173 D194 K230 K233 S234
Enzyme Commision number 6.1.1.1: tyrosine--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 485 A Y36 G38 A39 D40 H50 L70 D80 Y170 Q174 D177 G192 G193 D195 Q196 Y35 G37 A38 D39 H49 L69 D79 Y169 Q173 D176 G191 G192 D194 Q195 MOAD: ic50=4nM
PDBbind-CN: -logKd/Ki=8.40,IC50=4nM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003723 RNA binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004831 tyrosine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006437 tyrosyl-tRNA aminoacylation
GO:0043039 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:1jil, PDBe:1jil, PDBj:1jil
PDBsum1jil
PubMed11567092
UniProtA6QHR2|SYY_STAAE Tyrosine--tRNA ligase (Gene Name=tyrS)

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