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
PDB6cwj Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
ChainB
Resolution2.253 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)		 Binding affinity
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
External links
PDB RCSB:6cwj, PDBe:6cwj, PDBj:6cwj
PDBsum6cwj
PubMed31181074
UniProtQ2RGM7|CAH_MOOTA Cyanuric acid amidohydrolase (Gene Name=Moth_2120)

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