Structure of PDB 6buo Chain B

Receptor sequence

>6buoB (length=363) Species: 264732 (Moorella thermoacetica ATCC 39073)

HMQKVEVFRIPTASPDDISGLATLIDSGKINPAEIVAILGKTEGNGCVND
FTRGFATQSLAMYLAEKLGISREEVVKKVAFIMSGGTEGVMTPHITVFVR
KDVAAPAAPGKRLAVGVAFTRDFLPEELGRMEQVNEVARAVKEAMKDAQI
DDPRDVHFVQIKCPLLTAERIEDAKRRGKDVVVNDTYKSMAYSRGASALG
VALALGEISADKISNEAICHDWNLYSSVASTSAGVELLNDEIIVVGNSTN
SASDLVIGHSVMKDAIDADAVRAALKDAGIRSDDEMDRIVNVLAKAEAAS
SGTVRGRRNTMLDDSDINHTRSARAVVNAVIASVVGDPMVYVSGGAEHQG
PDGGGPIAVIARV

3D structure

• PDB: 6buo Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
• Chain: B
• Resolution: 1.85 Å

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	CA	B	E301 A350 Q353 G354 P355 G358	E297 A346 Q349 G350 P351 G354
BS02	PDO	B	E5 V6 F7	E6 V7 F8
BS03	PDO	B	K275 I279 D282 M290	K276 I280 D283 M286
BS04	PDO	B	W221 E301 D356	W222 E297 D352
BS05	PDO	B	R309 R311	R305 R307
BS06	PDO	B	Y186 N322	Y187 N318
BS07	PDO	B	K187 A190 H323 E351	K188 A191 H319 E347
BS08	PDO	B	N222 L223 Y224	N223 L224 Y225

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:6buo, PDBe:6buo, PDBj:6buo
• PDBsum: 6buo
• PubMed: 31181074
• UniProt: Q2RGM7|CAH_MOOTA Cyanuric acid amidohydrolase (Gene Name=Moth_2120)