Structure of PDB 3h0r Chain P

Receptor sequence
>3h0rP (length=478) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVKAYITPLYGKA
LKQAESLKERELPLFGIPIAVKDNILVEGEKTTCASKILENFVAPYDATV
IERLKKAGALIVGKTNLDEFAMGSSTEYSAFFPTKNPWDLERVPGGSSGG
SAASVAVLSAPVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA
SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPEWSEEVKKEVK
GLKIGLPKEFFEYELQPQVKEAFENFIKELEKEGFEIKEVSLPHVKYSIP
TYYIIAPSEASSNLARYDGVRYGYRAKEYKDIFEMYARTRDEGFGPEVKR
RIMLGTFALSAGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL
PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKDGLPVGGQLIG
KHWDETTLLQISYLWEQKFKHYEKIPLT
3D structure
PDB3h0r Insights into tRNA-Dependent Amidotransferase Evolution and Catalysis from the Structure of the Aquifex aeolicus Enzyme
ChainP
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K72 S147 S148 S166 T168 G169 G170 S171 Q174
Catalytic site (residue number reindexed from 1) K72 S147 S148 S166 T168 G169 G170 S171 Q174
Enzyme Commision number 6.3.5.7: glutaminyl-tRNA synthase (glutamine-hydrolyzing).
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 ASN P G123 T168 G169 S171 F199 Y302 R351 G123 T168 G169 S171 F199 Y302 R351
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
Cellular Component
GO:0030956 glutamyl-tRNA(Gln) amidotransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3h0r, PDBe:3h0r, PDBj:3h0r
PDBsum3h0r
PubMed19520089
UniProtO66610|GATA_AQUAE Glutamyl-tRNA(Gln) amidotransferase subunit A (Gene Name=gatA)

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