Structure of PDB 4nq3 Chain B

Receptor sequence
>4nq3B (length=347) Species: 438753 (Azorhizobium caulinodans ORS 571) [Search protein sequence]
MPIAKVHRIATASPDDVSGLAAAIATGAIAPAGILAIFGKTEGNGCVNDF
SRGFAVQSLQMLLRGHMGAAADEVCLVMSGGTEGGMSPHFLVFERAEPAL
AIGRAHTPDLPFEALGRMGQVRMVAQAVRRAMAAAGITDPEDVHFVQVKC
PLLTAMRVKEAEARGATTATSDTLKSMGLSRGASALGIALALGEVAEDAL
SDAVICADYGLWSARASCSSGIELLGHEIVVLGMSEGWSGPLAIAHGVMA
DAIDVTPVKAALSALGAEAGEATIVLAKAEPSRSGRIRGKRHTMLDDSDI
SPTRHARAFVAGALAGVVGHTEIYVSGGGEHQGPDGGGPVAVIAART
3D structure
PDB4nq3 Cyanuric acid hydrolase from Azorhizobium caulinodans ORS 571: crystal structure and insights into a new class of Ser-Lys dyad proteins.
ChainB
Resolution2.702 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.2.15: cyanuric acid amidohydrolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 BR8 B G45 R52 S79 G80 R188 S226 S227 R314 S333 G334 G45 R52 S79 G80 R181 S219 S220 R307 S326 G327
BS02 MG B E287 G336 Q339 G340 P341 G344 E280 G329 Q332 G333 P334 G337
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4nq3, PDBe:4nq3, PDBj:4nq3
PDBsum4nq3
PubMed24915109
UniProtA8IKD2|CAH_AZOC5 Cyanuric acid amidohydrolase (Gene Name=AZC_3892)

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