BioLiP

Structure of PDB 6cwj Chain B

Receptor sequence

>6cwjB (length=363) Species: 264732 (Moorella thermoacetica ATCC 39073) [Search protein sequence]

HMQKVEVFRIPTASPDDISGLATLIDSGKINPAEIVAILGKTEGNGCVND
FTRGFATQSLAMYLAEKLGISREEVVKKVAFIMSGGTEGVMTPHITVFVR
KDVAAPAAPGKRLAVGVAFTRDFLPEELGRMEQVNEVARAVKEAMKDAQI
DDPRDVHFVQIKCPLLTAERIEDAKRRGKDVVVNDTYKSMAYSRGASALG
VALALGEISADKISNEAICHDWNLYSSVASTSAGVELLNDEIIVVGNSTN
SASDLVIGHSVMKDAIDADAVRAALKDAGIRSDDEMDRIVNVLAKAEAAS
SGTVRGRRNTMLDDSDINHTRSARAVVNAVIASVVGDPMVYVSGGAEHQG
PDGGGPIAVIARV

3D structure

PDB

6cwj Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.

Chain

Resolution

2.253 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)
BS01	6JN	B	G45 R52 S83 G84 R193 S231 A232 R323 S342 G343	G46 R53 S84 G85 R194 S232 A233 R324 S343 G344
BS02	CA	B	E296 A345 Q348 G349 P350 G353	E297 A346 Q349 G350 P351 G354
BS03	PDO	B	A297 E346	A298 E347

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

PDB	RCSB:6cwj, PDBe:6cwj, PDBj:6cwj
PDBsum	6cwj
PubMed	31181074
UniProt	Q2RGM7\|CAH_MOOTA Cyanuric acid amidohydrolase (Gene Name=Moth_2120)