Structure of PDB 6bun Chain A

Receptor sequence
>6bunA (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.
ChainA
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 CA A E301 A350 Q353 G354 P355 G358 E296 A345 Q348 G349 P350 G353
BS02 PDO A D282 D283 D282 D283
BS03 PDO A W221 E301 W221 E296
BS04 PDO A G53 T56 Q57 G53 T56 Q57
BS05 PDO A D283 D291 D283 D286
BS06 CA A A107 G109 A107 G109
BS07 PDO A I321 A329 I316 A324
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:6bun, PDBe:6bun, PDBj:6bun
PDBsum6bun
PubMed31181074
UniProtQ2RGM7|CAH_MOOTA Cyanuric acid amidohydrolase (Gene Name=Moth_2120)

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