Structure of PDB 5lrt Chain A

Receptor sequence

>5lrtA (length=464) Species: 351607 (Acidothermus cellulolyticus 11B)

MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAPIGAPAQGLANVILT
NGARLYVDHAHPEYSTPEVTNPRDAVLWDKAGERIMAEAARRAADLPMGW
TIQLYKNNTDNKGASYGCHENYLMNRSTPFADIVRHLIPFFVTRQVFCGA
GRVGIGADGRGEGFQLSQRADFFEVEVGLETTLKRPIINTRDEPHADPEK
YRRLHVIIGDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVGAL
RAVSHDPTLRYQLRLHDGRRLTAVQLQMEYLEQARKYVEDRFGTDVDDMT
RDVLDRWETTLVRLADDPMQLSRDLDWVAKLSILEGYRQRENLPWSAHKL
QLVDLQYHDVRPDRGLYNRLVARGRMNLLVDEAAVRTAMHEPPNDTRAYF
RGRCLAKFGAEIAAASWDSVIFDLPGRDSLQRVPTLEPLRGTRAHVGDLL
DRCRSATELVAALT

3D structure

• PDB: 5lrt Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis.
• Chain: A
• Resolution: 1.85 Å

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	ADP	A	V4 G6 E8 R90 Y92 S101 T102 P103 E104 N157 L159 R227 R239 H241 W453	V4 G6 E8 R54 Y56 S65 T66 P67 E68 N121 L123 R191 R203 H205 W417
BS02	MG	A	E8 Y92 E99	E8 Y56 E63
BS03	MG	A	E8 H155 H241	E8 H119 H205
BS04	MG	A	E10 D94 E99	E10 D58 E63
BS05	PO4	A	E8 D94 E99 H155 R227 H241	E8 D58 E63 H119 R191 H205

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

External links

• PDB: RCSB:5lrt, PDBe:5lrt, PDBj:5lrt
• PDBsum: 5lrt
• PubMed: 28119453
• UniProt: A0LU48|DOP_ACIC1 Depupylase (Gene Name=dop)