Structure of PDB 6bup Chain A

Receptor sequence
>6bupA (length=361) Species: 264732 (Moorella thermoacetica ATCC 39073) [Search protein sequence]
HMQKVEVFRIPTASPDDISGLATLIDSGKINPAEIVAILGKTEGNGCVND
FTRGFATQSLAMYLAEKLGISREEVVKKVAFIMSGGTEGVMTPHITVFVR
KDVAAPPGKRLAVGVAFTRDFLPEELGRMEQVNEVARAVKEAMKDAQIDD
PRDVHFVQIKCPLLTAERIEDAKRRGKDVVVNDTYKSMAYSRGASALGVA
LALGEISADKISNEAICHDWNLYSSVASTSAGVELLNDEIIVVGNSTNSA
SDLVIGHSVMKDAIDADAVRAALKDAGIRSDDEMDRIVNVLAKAEAASSG
TVRGRRNTMLDDSDINHTRSARAVVNAVIASVVGDPMVYVSGGAEHQGPD
GGGPIAVIARV
3D structure
PDB6bup Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
ChainA
Resolution1.88 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 E295 A344 Q347 G348 P349 G352
BS02 PDO A E5 V6 E6 V7
BS03 PDO A K187 C218 W221 K186 C217 W220
BS04 PDO A H156 H258 D276 H155 H257 D275
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:6bup, PDBe:6bup, PDBj:6bup
PDBsum6bup
PubMed31181074
UniProtQ2RGM7|CAH_MOOTA Cyanuric acid amidohydrolase (Gene Name=Moth_2120)

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