Structure of PDB 3kfu Chain H

Receptor sequence
>3kfuH (length=467) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
LAHEIRARVARGEVSPLEVAQAYLKRVQELDPGLGAFLSLNERLLEEAEA
VDPGLPLAGLVVAVKDNIATRGLRTTAGSRLLENFVPPYEATAVARLKAL
GALVLGKTNLDEFGMGSSTEHSAFFPTKNPFDPDRVPGGSSGGSAAALAA
DLAPLALGSDTGGSVRQPAAFCGVYGLKPTYGRVSRFGLIAYASSLDQIG
PMARSVRDLALLMDAAAGPDPLDATSLDLPPRFQEALEGPLPPLRLGVVR
EALAGNSPGVERALEEALKVFRELGLSVREVSWPSLPQALAAYYILAPAE
ASSNLARYDGTLYGRRAAGEEVEGMMEATRALFGLEVKRRVLVGTFVLSS
GYYEAYYGRAQAFRRRLKAEAQALFREVDLLLLPTTPHPAFPFGARRDPL
AMYREDLYTVGANLTGLPALSFPAGFEGHLPVGLQLLAPWGEDERLLRAA
LAFEEATARAHLKAPLG
3D structure
PDB3kfu Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation.
ChainH
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) K66 S141 S142 S160 T162 G163 G164 S165 Q168
Catalytic site (residue number reindexed from 1) K65 S140 S141 S159 T161 G162 G163 S164 Q167
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 rna H G352 Y354 G351 Y353
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:3kfu, PDBe:3kfu, PDBj:3kfu
PDBsum3kfu
PubMed20717102
UniProtQ9LCX3|GATA_THET8 Glutamyl-tRNA(Gln) amidotransferase subunit A (Gene Name=gatA)

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