Structure of PDB 3h0l Chain H Binding Site BS02

Receptor Information

>3h0l Chain H (length=410) Species: 63363 (Aquifex aeolicus)

EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPVCLGMPGALPI
VNKRAVEYAIRASLALNCEVHEESVFARKHYFYPDLPKGYQISQYEKPLA
TNGWVELNLPNGEKKKVRIRRLHIEEDAGKNIHEGDKTLVDLNRAGTPLM
EIVTEPDIRTPEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP
KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGGEVVQETRTFD
PQTGKTYPMRTKEEAEDYRYFPDPDLVPLKVKKEWIEEIKKNMPELPDQR
FERLIKEYGLSEYEAGILVNHKEVGDFFEEAVRHFKEPKGIVNWLINDLL
GLLRDKGISIEESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT
PSQIVEEKGL

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 3h0l Chain H Residue 803

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3h0l Insights into tRNA-Dependent Amidotransferase Evolution and Catalysis from the Structure of the Aquifex aeolicus Enzyme
• Resolution: 2.3 Å
• Binding residue (original residue number in PDB): H14 E127 E153
• Binding residue (residue number reindexed from 1): H12 E125 E151
• Annotation score: 1

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

External links

• PDB: RCSB:3h0l, PDBe:3h0l, PDBj:3h0l
• PDBsum: 3h0l
• PubMed: 19520089
• UniProt: O66766|GATB_AQUAE Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)