Structure of PDB 3h0r Chain E Binding Site BS01

Receptor Information

>3h0r Chain E (length=410) Species: 63363 (Aquifex aeolicus)

EKYEAVIGLEIHVQMDTKTKMFCGCKVEFGAEPNTNVCPVCLGMPGALPI
VNKRAVEYAIRASLALNCEVHEESVFARKHYFYPDLPKGYQISQYEKPLA
TNGWVELNLPNGEKKKVRIRRLHIEEDAGKNIHEGDKTLVDLNRAGTPLM
EIVTEPDIRTPEEARLFLEKLRNIMRYAGVSKADMEKGQLRCDINVSIRP
KGSKEFGTRVEIKNVNSFRFVQKALEYEIERQINVVEEGGEVVQETRTFD
PQTGKTYPMRTKEEAEDYRYFPDPDLVPLKVKKEWIEEIKKNMPELPDQR
FERLIKEYGLSEYEAGILVNHKEVGDFFEEAVRHFKEPKGIVNWLINDLL
GLLRDKGISIEESPVKPEHLAELVKLIKEKVISTKIGKEVIKEMVETGKT
PSQIVEEKGL

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 3h0r Chain E Residue 902

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3h0r Insights into tRNA-Dependent Amidotransferase Evolution and Catalysis from the Structure of the Aquifex aeolicus Enzyme
• Resolution: 3.0 Å
• Binding residue (original residue number in PDB): C25 C27 C40 C43
• Binding residue (residue number reindexed from 1): C23 C25 C38 C41
• 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:3h0r, PDBe:3h0r, PDBj:3h0r
• PDBsum: 3h0r
• PubMed: 19520089
• UniProt: O66766|GATB_AQUAE Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)