Structure of PDB 4a91 Chain A

Receptor sequence
>4a91A (length=290) Species: 562 (Escherichia coli) [Search protein sequence]
DTQYIGRFAPSPSGELHFGSLIAALGSYLQARARQGRWLVRIEDIDPPRE
VPGAAETILRQLEHYGLHWDGDVLWQSQRHDAYREALAWLHEQGLSYYCT
CTRARIQSIGGIYDGHCRVLHHGPDNAAVRIRQQHPVTQFTDQLRGIIHA
DEKLAREDFIIHRRDGLFAYNLAVVVDDHFQGVTEIVRGADLIEPTVRQI
SLYQLFGWKVPDYIHLPLALNPQGAKLSKQAPALPKGDPRPVLIAALQFL
GQQAEAHWQDFSVEQILQSAVKNWRLTAVPESAIVNSTFS
3D structure
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.
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.-
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 GLU A R9 A11 S13 E45 Y172 R190 L194 R7 A9 S11 E43 Y170 R188 L192 MOAD: Kd=2.1mM
BS02 ZN A C101 C103 Y115 C119 C99 C101 Y113 C117
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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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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