Structure of PDB 6bum Chain C

Receptor sequence
>6bumC (length=363) Species: 264732 (Moorella thermoacetica ATCC 39073) [Search protein sequence]
HMQKVEVFRIPTASPDDISGLATLIDSGKINPAEIVAILGKTEGNGCVND
FTRGFATQSLAMYLAEKLGISREEVVKKVAFIMSGGTEGVMTPHITVFVR
KDVAAPAAPGKRLAVGVAFTRDFLPEELGRMEQVNEVARAVKEAMKDAQI
DDPRDVHFVQIKCPLLTAERIEDAKRRGKDVVVNDTYKSMAYSRGASALG
VALALGEISADKISNEAICHDWNLYSSVASTSAGVELLNDEIIVVGNSTN
SASDLVIGHSVMKDAIDADAVRAALKDAGIRSDDEMDRIVNVLAKAEAAS
SGTVRGRRNTMLDDSDINHTRSARAVVNAVIASVVGDPMVYVSGGAEHQG
PDGGGPIAVIARV
3D structure
PDB6bum Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
ChainC
Resolution1.51 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 C E301 A350 Q353 G354 P355 G358 E297 A346 Q349 G350 P351 G354
BS02 PDO C E5 V6 F7 E6 V7 F8
BS03 PDO C I321 S326 I317 S322
BS04 PDO C W221 E301 A350 E351 D356 W222 E297 A346 E347 D352
BS05 PDO C P152 R153 V155 E206 H258 P153 R154 V156 E207 H259
BS06 PDO C R271 I279 R272 I280
BS07 PDO C A267 R271 A268 R272
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:6bum, PDBe:6bum, PDBj:6bum
PDBsum6bum
PubMed31181074
UniProtQ2RGM7|CAH_MOOTA Cyanuric acid amidohydrolase (Gene Name=Moth_2120)

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