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- PDB-3m9d: Crystal structure of the prokaryotic ubiquintin-like protein Pup ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3m9d | ||||||
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Title | Crystal structure of the prokaryotic ubiquintin-like protein Pup complexed with the hexameric proteasomal ATPase Mpa which includes the amino terminal coiled coil domain and the inter domain | ||||||
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![]() | CHAPERONE / alpha helix coil coil / 5 beta-strand barrel / ATP-binding / Nucleotide-binding / Proteasome / S-nitrosylation / Virulence / Isopeptide bond / Ubl conjugation pathway | ||||||
Function / homology | ![]() ubiquitin-like protein reader activity / symbiont defense to host-produced reactive oxygen species / protein pupylation / proteasome-activating nucleotidase complex / symbiont-mediated perturbation of host defenses / response to nitrosative stress / cell wall / retrograde protein transport, ER to cytosol / ATP-dependent peptidase activity / proteasomal ubiquitin-independent protein catabolic process ...ubiquitin-like protein reader activity / symbiont defense to host-produced reactive oxygen species / protein pupylation / proteasome-activating nucleotidase complex / symbiont-mediated perturbation of host defenses / response to nitrosative stress / cell wall / retrograde protein transport, ER to cytosol / ATP-dependent peptidase activity / proteasomal ubiquitin-independent protein catabolic process / proteasome binding / protein unfolding / cellular response to nitric oxide / polyubiquitin modification-dependent protein binding / proteasomal protein catabolic process / peptidoglycan-based cell wall / modification-dependent protein catabolic process / protein tag activity / molecular adaptor activity / ATP hydrolysis activity / ATP binding / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Li, H. / Wang, T. | ||||||
![]() | ![]() Title: Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. Authors: Wang, T. / Darwin, K.H. / Li, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 937.2 KB | Display | ![]() |
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PDB format | ![]() | 792 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 621.9 KB | Display | ![]() |
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Full document | ![]() | 754.2 KB | Display | |
Data in XML | ![]() | 94.6 KB | Display | |
Data in CIF | ![]() | 126.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Refine code: 2
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