2F6I

Crystal structure of the ClpP protease catalytic domain from Plasmodium falciparum

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2f6ia1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
A	d2f6ia2	Artifacts	Tags	Tags	Tags	N-terminal Tags	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
B	d2f6ib2	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
B	d2f6ib3	Artifacts	Tags	Tags	Tags	N-terminal Tags	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
C	d2f6ic2	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
C	d2f6ic3	Artifacts	Tags	Tags	Tags	N-terminal Tags	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
E	d2f6ie2	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
E	d2f6ie3	Artifacts	Tags	Tags	Tags	N-terminal Tags	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
D	d2f6id2	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
D	d2f6id3	Artifacts	Tags	Tags	Tags	N-terminal Tags	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
F	d2f6if2	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
F	d2f6if3	Artifacts	Tags	Tags	Tags	N-terminal Tags	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
G	d2f6ig2	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	Clp protease, ClpP subunit	Clp protease, ClpP subunit	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)
G	d2f6ig3	Artifacts	Tags	Tags	Tags	N-terminal Tags	malaria parasite P. falciparum (Plasmodium falciparum ) [TaxId: 5833 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Clp protease ClpP subunit	8028198	4003574	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ClpP/crotonase	8040577	3000033	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	ClpP/crotonase	8040577	3000033	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ClpP/crotonase	8040577	3000033	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	ClpP/crotonase	8040577	3000033	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ClpP/crotonase	8040577	3000033	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	ClpP/crotonase	8040577	3000033	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	ClpP/crotonase	8040577	3000033	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)
A	PF00574	e2f6iA1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00574	ECOD (1.6)
B	PF00574	e2f6iB1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00574	ECOD (1.6)
C	PF00574	e2f6iC1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00574	ECOD (1.6)
E	PF00574	e2f6iE1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00574	ECOD (1.6)
D	PF00574	e2f6iD1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00574	ECOD (1.6)
F	PF00574	e2f6iF1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00574	ECOD (1.6)
G	PF00574	e2f6iG1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: PF00574	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
B	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
C	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
E	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
D	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
F	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
G	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G	PF00574	Clp protease (CLP_protease)	Clp protease	The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large in ...	The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large insertions, Swiss:P42380 contains one large insertion.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G	ATP-dependent CLP protease, putative	hydrolase activity catalytic activity peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity ATP-dependent peptidase activity ATP-dependent activity ATPase binding protein binding binding enzyme binding	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process organonitrogen compound catabolic process catabolic process proteolysis involved in protein catabolic process protein catabolic process macromolecule catabolic process protein quality control for misfolded or incompletely synthesized proteins organic substance catabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure plastid organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle apicoplast endopeptidase Clp complex protein-containing complex catalytic complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G	IPR001907	ATP-dependent Clp protease proteolytic subunit	Family
A, B, C, D, E A, B, C, D, E, F, G	IPR033135	ClpP, histidine active site	Active Site
A, B, C, D, E A, B, C, D, E, F, G	IPR023562	Clp protease proteolytic subunit /Translocation-enhancing protein TepA	Family

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 R01GM133198.