Structure of PDB 5lrt Chain A Binding Site BS02

Receptor Information

>5lrt Chain A (length=464) Species: 351607 (Acidothermus cellulolyticus 11B)

MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAPIGAPAQGLANVILT
NGARLYVDHAHPEYSTPEVTNPRDAVLWDKAGERIMAEAARRAADLPMGW
TIQLYKNNTDNKGASYGCHENYLMNRSTPFADIVRHLIPFFVTRQVFCGA
GRVGIGADGRGEGFQLSQRADFFEVEVGLETTLKRPIINTRDEPHADPEK
YRRLHVIIGDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVGAL
RAVSHDPTLRYQLRLHDGRRLTAVQLQMEYLEQARKYVEDRFGTDVDDMT
RDVLDRWETTLVRLADDPMQLSRDLDWVAKLSILEGYRQRENLPWSAHKL
QLVDLQYHDVRPDRGLYNRLVARGRMNLLVDEAAVRTAMHEPPNDTRAYF
RGRCLAKFGAEIAAASWDSVIFDLPGRDSLQRVPTLEPLRGTRAHVGDLL
DRCRSATELVAALT

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 5lrt Chain A Residue 603

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5lrt Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis.
• Resolution: 1.85 Å
• Binding residue (original residue number in PDB): E8 Y92 E99
• Binding residue (residue number reindexed from 1): E8 Y56 E63
• Annotation score: 4

Enzymatic activity

• Enzyme Commision number: 3.4.-.-

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)