Structure of PDB 4nq3 Chain B Binding Site BS02

Receptor Information

>4nq3 Chain B (length=347) Species: 438753 (Azorhizobium caulinodans ORS 571)

MPIAKVHRIATASPDDVSGLAAAIATGAIAPAGILAIFGKTEGNGCVNDF
SRGFAVQSLQMLLRGHMGAAADEVCLVMSGGTEGGMSPHFLVFERAEPAL
AIGRAHTPDLPFEALGRMGQVRMVAQAVRRAMAAAGITDPEDVHFVQVKC
PLLTAMRVKEAEARGATTATSDTLKSMGLSRGASALGIALALGEVAEDAL
SDAVICADYGLWSARASCSSGIELLGHEIVVLGMSEGWSGPLAIAHGVMA
DAIDVTPVKAALSALGAEAGEATIVLAKAEPSRSGRIRGKRHTMLDDSDI
SPTRHARAFVAGALAGVVGHTEIYVSGGGEHQGPDGGGPVAVIAART

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: 4nq3 Chain B Residue 406

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4nq3 Cyanuric acid hydrolase from Azorhizobium caulinodans ORS 571: crystal structure and insights into a new class of Ser-Lys dyad proteins.
• Resolution: 2.702 Å
• Binding residue (original residue number in PDB): E287 G336 Q339 G340 P341 G344
• Binding residue (residue number reindexed from 1): E280 G329 Q332 G333 P334 G337
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.5.2.15: cyanuric acid amidohydrolase.

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
• GO:0018753 cyanuric acid amidohydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0019381 atrazine catabolic process

External links

• PDB: RCSB:4nq3, PDBe:4nq3, PDBj:4nq3
• PDBsum: 4nq3
• PubMed: 24915109
• UniProt: A8IKD2|CAH_AZOC5 Cyanuric acid amidohydrolase (Gene Name=AZC_3892)