Structure of PDB 3h0l Chain Q

Receptor sequence
>3h0lQ (length=410) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPVCLGMPGALPI
VNKRAVEYAIRASLALNCEVHEESVFARKHYFYPDLPKGYQISQYEKPLA
TNGWVELNLPNGEKKKVRIRRLHIEEDAGKNIHEGDKTLVDLNRAGTPLM
EIVTEPDIRTPEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP
KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGGEVVQETRTFD
PQTGKTYPMRTKEEAEDYRYFPDPDLVPLKVKKEWIEEIKKNMPELPDQR
FERLIKEYGLSEYEAGILVNHKEVGDFFEEAVRHFKEPKGIVNWLINDLL
GLLRDKGISIEESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT
PSQIVEEKGL
3D structure
PDB3h0l Insights into tRNA-Dependent Amidotransferase Evolution and Catalysis from the Structure of the Aquifex aeolicus Enzyme
ChainQ
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.5.-
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 ADP Q V8 G10 L11 E12 V155 T156 P158 N197 V198 S199 R211 V6 G8 L9 E10 V153 T154 P156 N195 V196 S197 R209
BS02 MG Q H14 E127 E153 H12 E125 E151
BS03 ZN Q C25 C27 C40 C43 C23 C25 C38 C41
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016884 carbon-nitrogen ligase activity, with glutamine as amido-N-donor
GO:0050566 asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
GO:0070681 glutaminyl-tRNAGln biosynthesis via transamidation

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Molecular Function
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Biological Process
External links
PDB RCSB:3h0l, PDBe:3h0l, PDBj:3h0l
PDBsum3h0l
PubMed19520089
UniProtO66766|GATB_AQUAE Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)

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