4CAB

The refined structure of catalase DR1998 from Deinococcus radiodurans at 2.6 A resolution

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	d4caba_	Multi-domain proteins (alpha and beta)	Heme-dependent catalase-like	Heme-dependent catalase-like	automated matches	automated matches	(Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 ) [TaxId: 243230 ],	SCOPe (2.08)
B	d4cabb_	Multi-domain proteins (alpha and beta)	Heme-dependent catalase-like	Heme-dependent catalase-like	automated matches	automated matches	(Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 ) [TaxId: 243230 ],	SCOPe (2.08)
C	d4cabc_	Multi-domain proteins (alpha and beta)	Heme-dependent catalase-like	Heme-dependent catalase-like	automated matches	automated matches	(Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 ) [TaxId: 243230 ],	SCOPe (2.08)
D	d4cabd_	Multi-domain proteins (alpha and beta)	Heme-dependent catalase-like	Heme-dependent catalase-like	automated matches	automated matches	(Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 ) [TaxId: 243230 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Heme-dependent catalases	8068992	4002736	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Heme-dependent catalase-like	8068993	3001681	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Heme-dependent catalase-like	8068993	3001681	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Heme-dependent catalase-like	8068993	3001681	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Heme-dependent catalase-like	8068993	3001681	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	Catalase	e4cabA1	A: beta barrels	X: Barrel domain in heme-dependent catalases (From Topology)	H: Barrel domain in heme-dependent catalases (From Topology)	T: Barrel domain in heme-dependent catalases	F: Catalase	ECOD (1.6)
A	Catalase_1	e4cabA2	A: alpha bundles	X: First alpha-helical domain in heme-dependent catalases (From Topology)	H: First alpha-helical domain in heme-dependent catalases (From Topology)	T: First alpha-helical domain in heme-dependent catalases	F: Catalase_1	ECOD (1.6)
A	Catalase-rel	e4cabA3	A: alpha bundles	X: Second alpha-helical domain in heme-dependent catalases (From Topology)	H: Second alpha-helical domain in heme-dependent catalases (From Topology)	T: Second alpha-helical domain in heme-dependent catalases	F: Catalase-rel	ECOD (1.6)
B	Catalase	e4cabB1	A: beta barrels	X: Barrel domain in heme-dependent catalases (From Topology)	H: Barrel domain in heme-dependent catalases (From Topology)	T: Barrel domain in heme-dependent catalases	F: Catalase	ECOD (1.6)
B	Catalase_1	e4cabB2	A: alpha bundles	X: First alpha-helical domain in heme-dependent catalases (From Topology)	H: First alpha-helical domain in heme-dependent catalases (From Topology)	T: First alpha-helical domain in heme-dependent catalases	F: Catalase_1	ECOD (1.6)
B	Catalase-rel	e4cabB3	A: alpha bundles	X: Second alpha-helical domain in heme-dependent catalases (From Topology)	H: Second alpha-helical domain in heme-dependent catalases (From Topology)	T: Second alpha-helical domain in heme-dependent catalases	F: Catalase-rel	ECOD (1.6)
C	Catalase	e4cabC1	A: beta barrels	X: Barrel domain in heme-dependent catalases (From Topology)	H: Barrel domain in heme-dependent catalases (From Topology)	T: Barrel domain in heme-dependent catalases	F: Catalase	ECOD (1.6)
C	Catalase_1	e4cabC2	A: alpha bundles	X: First alpha-helical domain in heme-dependent catalases (From Topology)	H: First alpha-helical domain in heme-dependent catalases (From Topology)	T: First alpha-helical domain in heme-dependent catalases	F: Catalase_1	ECOD (1.6)
C	Catalase-rel	e4cabC3	A: alpha bundles	X: Second alpha-helical domain in heme-dependent catalases (From Topology)	H: Second alpha-helical domain in heme-dependent catalases (From Topology)	T: Second alpha-helical domain in heme-dependent catalases	F: Catalase-rel	ECOD (1.6)
D	Catalase	e4cabD1	A: beta barrels	X: Barrel domain in heme-dependent catalases (From Topology)	H: Barrel domain in heme-dependent catalases (From Topology)	T: Barrel domain in heme-dependent catalases	F: Catalase	ECOD (1.6)
D	Catalase_1	e4cabD2	A: alpha bundles	X: First alpha-helical domain in heme-dependent catalases (From Topology)	H: First alpha-helical domain in heme-dependent catalases (From Topology)	T: First alpha-helical domain in heme-dependent catalases	F: Catalase_1	ECOD (1.6)
D	Catalase-rel	e4cabD3	A: alpha bundles	X: Second alpha-helical domain in heme-dependent catalases (From Topology)	H: Second alpha-helical domain in heme-dependent catalases (From Topology)	T: Second alpha-helical domain in heme-dependent catalases	F: Catalase-rel	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.180.10	Mainly Beta	Beta Barrel	Catalase HpII, Chain A, domain 1	Catalase core domain	CATH (4.3.0)
B	2.40.180.10	Mainly Beta	Beta Barrel	Catalase HpII, Chain A, domain 1	Catalase core domain	CATH (4.3.0)
C	2.40.180.10	Mainly Beta	Beta Barrel	Catalase HpII, Chain A, domain 1	Catalase core domain	CATH (4.3.0)
D	2.40.180.10	Mainly Beta	Beta Barrel	Catalase HpII, Chain A, domain 1	Catalase core domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF06628	Catalase-related immune-responsive (Catalase-rel)	Catalase-related immune-responsive	-	Family
A, B, C, D	PF00199	Catalase (Catalase)	Catalase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	CATALASE	peroxidase activity oxidoreductase activity antioxidant activity catalase activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding small molecule binding	cellular catabolic process catabolic process cellular metabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process response to hydrogen peroxide response to oxidative stress response to stimulus response to stress response to chemical response to oxygen-containing compound cellular catabolic process catabolic process cellular metabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process response to hydrogen peroxide response to oxidative stress response to stimulus response to stress response to chemical response to oxygen-containing compound response to reactive oxygen species response to inorganic substance	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR024711	Catalase, mono-functional, haem-containing, clades 1 and 3	Family
A, B, C, D	IPR011614	Catalase core domain	Domain
A, B, C, D	IPR018028	Catalase, mono-functional, haem-containing	Family
A, B, C, D	IPR010582	Catalase immune-responsive domain	Domain
A, B, C, D	IPR002226	Catalase haem-binding site	Binding Site
A, B, C, D	IPR020835	Catalase superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.