Structure of PDB 6bup Chain D

Receptor sequence
>6bupD (length=362) Species: 264732 (Moorella thermoacetica ATCC 39073) [Search protein sequence]
MQKVEVFRIPTASPDDISGLATLIDSGKINPAEIVAILGKTEGNGCVNDF
TRGFATQSLAMYLAEKLGISREEVVKKVAFIMSGGTEGVMTPHITVFVRK
DVAAPAAPGKRLAVGVAFTRDFLPEELGRMEQVNEVARAVKEAMKDAQID
DPRDVHFVQIKCPLLTAERIEDAKRRGKDVVVNDTYKSMAYSRGASALGV
ALALGEISADKISNEAICHDWNLYSSVASTSAGVELLNDEIIVVGNSTNS
ASDLVIGHSVMKDAIDADAVRAALKDAGIRSDDEMDRIVNVLAKAEAASS
GTVRGRRNTMLDDSDINHTRSARAVVNAVIASVVGDPMVYVSGGAEHQGP
DGGGPIAVIARV
3D structure
PDB6bup Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
ChainD
Resolution1.88 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D E301 A350 Q353 G354 P355 D356 G358 E296 A345 Q348 G349 P350 D351 G353
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6bup, PDBe:6bup, PDBj:6bup
PDBsum6bup
PubMed31181074
UniProtQ2RGM7|CAH_MOOTA Cyanuric acid amidohydrolase (Gene Name=Moth_2120)

[Back to BioLiP]