6X1M

Lon protease proteolytic domain complexed with covalent boronic acid inhibitor

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8075401	3000100	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8075401	3000100	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8075401	3000100	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Lon_C_N	e6x1mB2	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
B	Lon_C_C	e6x1mB1	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)
A	Lon_C_N	e6x1mA1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
A	Lon_C_C	e6x1mA2	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)
C	Lon_C_N	e6x1mC2	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
C	Lon_C_C	e6x1mC1	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF05362	Lon protease (S16) C-terminal proteolytic domain (Lon_C)	Lon protease (S16) C-terminal proteolytic domain	The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activit ...	The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Lon protease homolog, mitochondrial	PH domain binding protein binding binding protein domain specific binding insulin receptor substrate binding RNA binding organic cyclic compound binding nucleic acid binding single-stranded RNA binding peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity PH domain binding protein binding binding protein domain specific binding insulin receptor substrate binding RNA binding organic cyclic compound binding nucleic acid binding single-stranded RNA binding peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity DNA binding G-quadruplex DNA binding sequence-specific DNA binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding ADP binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity, acting on acid anhydrides ATP-dependent activity ATP-dependent peptidase activity DNA polymerase binding enzyme binding identical protein binding single-stranded DNA binding	cellular component organization cellular component biogenesis cellular component assembly chaperone-mediated protein complex assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis catabolic process mitochondrial protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organelle organization cellular component organization cellular component biogenesis cellular component assembly chaperone-mediated protein complex assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis catabolic process mitochondrial protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organelle organization metabolic process protein metabolic process macromolecule metabolic process mitochondrion organization proteolysis involved in protein catabolic process proteolysis cellular response to stimulus response to oxidative stress cellular response to chemical stimulus response to stimulus cellular response to stress response to stress response to chemical cellular response to oxidative stress cellular response to chemical stress cellular response to nitrogen compound regulation of cellular process negative regulation of signaling signaling response to peptide hormone negative regulation of biological process regulation of signal transduction insulin receptor signaling pathway regulation of cellular response to insulin stimulus negative regulation of cell communication cell surface receptor protein tyrosine kinase signaling pathway cell communication cellular response to endogenous stimulus response to hormone negative regulation of cellular process signal transduction enzyme-linked receptor protein signaling pathway cellular response to hormone stimulus regulation of signaling regulation of biological process cell surface receptor signaling pathway negative regulation of response to stimulus response to endogenous stimulus regulation of insulin receptor signaling pathway biological regulation response to oxygen-containing compound cellular response to peptide hormone stimulus response to nitrogen compound negative regulation of signal transduction cellular response to oxygen-containing compound negative regulation of cellular response to insulin stimulus regulation of response to stimulus negative regulation of insulin receptor signaling pathway response to insulin regulation of cell communication cellular response to insulin stimulus mitochondrial genome maintenance response to decreased oxygen levels response to hypoxia response to oxygen levels response to abiotic stimulus modification-dependent macromolecule catabolic process modification-dependent protein catabolic process oxidation-dependent protein catabolic process DNA metabolic process nucleic acid metabolic process mitochondrial DNA metabolic process nucleobase-containing compound metabolic process protein quality control for misfolded or incompletely synthesized proteins	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle membrane cytosol nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle membrane cytosol nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen intracellular membraneless organelle nucleoid mitochondrial matrix membraneless organelle mitochondrial nucleoid

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR015947	PUA-like superfamily	Homologous Superfamily
A, B, C	IPR046336	Lon protease, N-terminal domain superfamily	Homologous Superfamily
A, B, C	IPR003593	AAA+ ATPase domain	Domain
A, B, C	IPR027065	Lon protease	Family
A, B, C	IPR008268	Peptidase S16, active site	Active Site
A, B, C	IPR003959	ATPase, AAA-type, core	Domain
A, B, C	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A, B, C	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, B, C	IPR014721	Small ribosomal subunit protein uS5 domain 2-type fold, subgroup	Homologous Superfamily
A, B, C	IPR003111	Lon protease, N-terminal domain	Domain
A, B, C	IPR004815	Lon protease, bacterial/eukaryotic-type	Family
A, B, C	IPR054594	Lon protease, AAA+ ATPase lid domain	Domain
A, B, C	IPR008269	Peptidase S16, Lon proteolytic domain	Domain
A, B, C	IPR027503	Lon protease homologue, chloroplastic/mitochondrial	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C	Pharos: P36776	CODAS syndrome cataract intellectual disability psoriasis Mitochondrial Diseases diabetes mellitus ovarian cancer

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.