Structure of PDB 4b0s Chain A

Receptor sequence
>4b0sA (length=456) Species: 351607 (Acidothermus cellulolyticus 11B) [Search protein sequence]
MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAPANVILTNGARLYVD
HAHPEYSTPEVTNPRDAVLWDKAGERIMAEAARRAADLPMGWTIQLYKNN
TDNKGASYGCHENYLMNRSTPFADIVRHLIPFFVTRQVFCGAGRVGIGAD
GRGEGFQLSQRADFFEVEVGLETTLKRPIINTRDEPHADPEKYRRLHVII
GDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVGALRAVSHDPT
LRYQLRLHDGRRLTAVQLQMEYLEQARKYVEDRFGTDVDDMTRDVLDRWE
TTLVRLADDPMQLSRDLDWVAKLSILEGYRQRENLPWSAHKLQLVDLQYH
DVRPDRGLYNRLVARGRMNLLVDEAAVRTAMHEPPNDTRAYFRGRCLAKF
GAEIAAASWDSVIFDLPGRDSLQRVPTLEPLRGTRAHVGDLLDRCRSATE
LVAALT
3D structure
PDB4b0s Structures of Pup Ligase Pafa and Depupylase Dop from the Prokaryotic Ubiquitin-Like Modification Pathway.
ChainA
Resolution2.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.-.-
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 ATP A G6 I7 E8 R90 Y92 E99 S101 T102 N157 L159 P230 R239 W453 G6 I7 E8 R46 Y48 E55 S57 T58 N113 L115 P186 R195 W409
BS02 MG A E8 H155 H241 E8 H111 H197
BS03 MG A E8 Y92 E99 E8 Y48 E55
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:4b0s, PDBe:4b0s, PDBj:4b0s
PDBsum4b0s
PubMed22910360
UniProtA0LU48|DOP_ACIC1 Depupylase (Gene Name=dop)

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