Structure of PDB 7oy3 Chain A

Receptor sequence
>7oy3A (length=471) Species: 28049 (Acidothermus cellulolyticus) [Search protein sequence]
MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAQARWDFGLANVILTN
GARLYVDHAHPEYSTPEVTNPRDAVLWDKAGERIMAEAARRAADLPMGWT
IQLYKNNTDNKGASYGCHENYLMNRSTPFADIVRHLIPFFVTRQVFCGAG
RVGIGADGRGEGFQLSQRADFFEVEVGLETTLKRPIINTRDEPHADPEKY
RRLHVIIGDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVGALR
AVSHDPTLRYQLRLHDGRRLTAVQLQMEYLEQARKYVEDRFGTDVDDMTR
DVLDRWETTLVRLADDPMQLSRDLDWVAKLSILEGYRQRENLPWSAHKLQ
LVDLQYHDVRPDRGLYNRLVARGRMNLLVDEAAVRTAMHEPPNDTRAYFR
GRCLAKFGAEIAAASWDSVIFDLPGRDSLQRVPTLEPLRGTRAHVGDLLD
RCRSATELVAALTGGENLYFQ
3D structure
PDB7oy3 Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation.
ChainA
Resolution1.78 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.-.-
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008233 peptidase activity
GO:0016787 hydrolase activity
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO:0046872 metal ion binding
Biological Process
GO:0010498 proteasomal protein catabolic process
GO:0019941 modification-dependent protein catabolic process
GO:0070490 protein pupylation

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Molecular Function
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Biological Process
External links
PDB RCSB:7oy3, PDBe:7oy3, PDBj:7oy3
PDBsum7oy3
PubMed34789727
UniProtA0LU48|DOP_ACIC1 Depupylase (Gene Name=dop)

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