Structure of PDB 6bun Chain D

Receptor sequence
>6bunD (length=362) Species: 264732 (Moorella thermoacetica ATCC 39073) [Search protein sequence]
MQKVEVFRIPTASPDDISGLATLIDSGKINPAEIVAILGKTEGNGCVNDF
TRGFATQSLAMYLAEKLGISREEVVKKVAFIMSGGTEGVMTPHITVFVRK
DVAAPAAPGKRLAVGVAFTRDFLPEELGRMEQVNEVARAVKEAMKDAQID
DPRDVHFVQIKCPLLTAERIEDAKRRGKDVVVNDTYKSMAYSRGASALGV
ALALGEISADKISNEAICHDWNLYSSVASTSAGVELLNDEIIVVGNSTNS
ASDLVIGHSVMKDAIDADAVRAALKDAGIRSDDEMDRIVNVLAKAEAASS
GTVRGRRNTMLDDSDINHTRSARAVVNAVIASVVGDPMVYVSGGAEHQGP
DGGGPIAVIARV
3D structure
PDB6bun Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
ChainD
Resolution1.78 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 PDO D S13 D15 S13 D15
BS02 CA D E301 A350 Q353 G354 P355 G358 E296 A345 Q348 G349 P350 G353
BS03 PDO D N222 L223 Y224 N222 L223 Y224
BS04 PDO D V47 D49 F50 V47 D49 F50
BS05 PDO D E5 V6 F7 E5 V6 F7
BS06 PDO D I321 S326 I316 S321
BS07 PDO D G348 G349 G343 G344
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
View graph for
Biological Process
External links
PDB RCSB:6bun, PDBe:6bun, PDBj:6bun
PDBsum6bun
PubMed31181074
UniProtQ2RGM7|CAH_MOOTA Cyanuric acid amidohydrolase (Gene Name=Moth_2120)

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