Structure of PDB 3h0r Chain M Binding Site BS01

Receptor Information
>3h0r Chain M (length=478) Species: 63363 (Aquifex aeolicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVKAYITPLYGKA
LKQAESLKERELPLFGIPIAVKDNILVEGEKTTCASKILENFVAPYDATV
IERLKKAGALIVGKTNLDEFAMGSSTEYSAFFPTKNPWDLERVPGGSSGG
SAASVAVLSAPVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA
SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPEWSEEVKKEVK
GLKIGLPKEFFEYELQPQVKEAFENFIKELEKEGFEIKEVSLPHVKYSIP
TYYIIAPSEASSNLARYDGVRYGYRAKEYKDIFEMYARTRDEGFGPEVKR
RIMLGTFALSAGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL
PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKDGLPVGGQLIG
KHWDETTLLQISYLWEQKFKHYEKIPLT
Ligand information
Ligand IDASN
InChIInChI=1S/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1
InChIKeyDCXYFEDJOCDNAF-REOHCLBHSA-N
SMILES
SoftwareSMILES
CACTVS 3.370N[C@@H](CC(N)=O)C(O)=O
ACDLabs 12.01O=C(N)CC(N)C(=O)O
CACTVS 3.370N[CH](CC(N)=O)C(O)=O
OpenEye OEToolkits 1.7.2C(C(C(=O)O)N)C(=O)N
OpenEye OEToolkits 1.7.2C([C@@H](C(=O)O)N)C(=O)N
FormulaC4 H8 N2 O3
NameASPARAGINE
ChEMBLCHEMBL58832
DrugBankDB00174
ZINCZINC000001532556
PDB chain3h0r Chain M Residue 905 [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)		A121 T168 G169 S171 F199 Y302 Y303 R351 D418
Binding residue
(residue number reindexed from 1)		A121 T168 G169 S171 F199 Y302 Y303 R351 D418
Annotation score3
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).
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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