Structure of PDB 4a91 Chain A Binding Site BS02

Receptor Information
>4a91 Chain A (length=290) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DTQYIGRFAPSPSGELHFGSLIAALGSYLQARARQGRWLVRIEDIDPPRE
VPGAAETILRQLEHYGLHWDGDVLWQSQRHDAYREALAWLHEQGLSYYCT
CTRARIQSIGGIYDGHCRVLHHGPDNAAVRIRQQHPVTQFTDQLRGIIHA
DEKLAREDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQI
SLYQLFGWKVPDYIHLPLALNPQGAKLSKQAPALPKGDPRPVLIAALQFL
GQQAEAHWQDFSVEQILQSAVKNWRLTAVPESAIVNSTFS
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4a91 Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4a91 Crystal Structure of Glutamyl-Queuosine Trnaasp Synthetase Complexed with L-Glutamate: Structural Elements Mediating tRNA-Independent Activation of Glutamate and Glutamylation of Trnaasp Anticodon.
Resolution1.75 Å
Binding residue
(original residue number in PDB)		C101 C103 Y115 C119
Binding residue
(residue number reindexed from 1)		C99 C101 Y113 C117
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S13 K231
Catalytic site (residue number reindexed from 1) S11 K229
Enzyme Commision number 6.1.1.-
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004818 glutamate-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0002097 tRNA wobble base modification
GO:0006400 tRNA modification
GO:0006424 glutamyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
Cellular Component
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:4a91, PDBe:4a91, PDBj:4a91
PDBsum4a91
PubMed18602926
UniProtP27305|GLUQ_ECOLI Glutamyl-Q tRNA(Asp) synthetase (Gene Name=gluQ)

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