Structure of PDB 6bqz Chain A Binding Site BS02

Receptor Information
>6bqz Chain A (length=215) Species: 470 (Acinetobacter baumannii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HHHLPAEEQLALIQRGTHEIISEEDLLKKLKENRPLKIKAGFDPTAPDLH
LGHTVLINKLKTFQDLGHEVTFLIGDYTAMIGDPTRPPLSREQVEANAKT
YQEQVFKILDPNKTKVRFNSEWFNQKSAADLIQLASQQTVSRMLERDDFT
KRYNNHQPIAIHEFLYPLVQGYDSIALEADVELGGTDQTFNLLMGRTLQS
RYGQESQVCITVPIL
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain6bqz Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6bqz Crystal Structure of Tyrosine-tRNA Synthetase from Acinetobacter baumannii with bound L-Tyrosine
Resolution2.3 Å
Binding residue
(original residue number in PDB)
R129 F130 E133
Binding residue
(residue number reindexed from 1)
R117 F118 E121
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T52 H57 H60 R98 Q182 D199
Catalytic site (residue number reindexed from 1) T45 H50 H53 R86 Q170 D187
Enzyme Commision number 6.1.1.1: tyrosine--tRNA ligase.
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
GO:0046872 metal ion 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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Biological Process

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Cellular Component
External links
PDB RCSB:6bqz, PDBe:6bqz, PDBj:6bqz
PDBsum6bqz
PubMed
UniProtB0VML7

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