Structure of PDB 3h0r Chain N Binding Site BS05

Receptor Information
>3h0r Chain N (length=410) Species: 63363 (Aquifex aeolicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPVCLGMPGALPI
VNKRAVEYAIRASLALNCEVHEESVFARKHYFYPDLPKGYQISQYEKPLA
TNGWVELNLPNGEKKKVRIRRLHIEEDAGKNIHEGDKTLVDLNRAGTPLM
EIVTEPDIRTPEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP
KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGGEVVQETRTFD
PQTGKTYPMRTKEEAEDYRYFPDPDLVPLKVKKEWIEEIKKNMPELPDQR
FERLIKEYGLSEYEAGILVNHKEVGDFFEEAVRHFKEPKGIVNWLINDLL
GLLRDKGISIEESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT
PSQIVEEKGL
Ligand information
Ligand IDASP
InChIInChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1
InChIKeyCKLJMWTZIZZHCS-REOHCLBHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C(C(C(=O)O)N)C(=O)O
OpenEye OEToolkits 1.7.0C([C@@H](C(=O)O)N)C(=O)O
CACTVS 3.370N[CH](CC(O)=O)C(O)=O
CACTVS 3.370N[C@@H](CC(O)=O)C(O)=O
ACDLabs 12.01O=C(O)CC(N)C(=O)O
FormulaC4 H7 N O4
NameASPARTIC ACID
ChEMBLCHEMBL274323
DrugBankDB00128
ZINCZINC000000895032
PDB chain3h0r Chain N Residue 482 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3h0r Insights into tRNA-Dependent Amidotransferase Evolution and Catalysis from the Structure of the Aquifex aeolicus Enzyme
Resolution3.0 Å
Binding residue
(original residue number in PDB)		K81 E153
Binding residue
(residue number reindexed from 1)		K79 E151
Annotation score3
Enzymatic activity
Enzyme Commision number 6.3.5.-
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:3h0r, PDBe:3h0r, PDBj:3h0r
PDBsum3h0r
PubMed19520089
UniProtO66766|GATB_AQUAE Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)

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