4E37

Crystal Structure of P. aeruginosa catalase, KatA tetramer

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
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4e37a_	Multi-domain proteins (alpha and beta)	Heme-dependent catalase-like	Heme-dependent catalase-like	Heme-dependent catalases	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)
B	d4e37b_	Multi-domain proteins (alpha and beta)	Heme-dependent catalase-like	Heme-dependent catalase-like	Heme-dependent catalases	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)
C	d4e37c_	Multi-domain proteins (alpha and beta)	Heme-dependent catalase-like	Heme-dependent catalase-like	Heme-dependent catalases	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)
D	d4e37d_	Multi-domain proteins (alpha and beta)	Heme-dependent catalase-like	Heme-dependent catalase-like	Heme-dependent catalases	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	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	8068986	4002736	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Heme-dependent catalase-like	8068987	3001681	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Heme-dependent catalase-like	8068987	3001681	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Heme-dependent catalase-like	8068987	3001681	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Heme-dependent catalase-like	8068987	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	PF00199	e4e37A3	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: PF00199	ECOD (1.6)
A	PF00199	e4e37A1	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: PF00199	ECOD (1.6)
A	PF06628	e4e37A2	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: PF06628	ECOD (1.6)
B	PF00199	e4e37B1	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: PF00199	ECOD (1.6)
B	PF00199	e4e37B3	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: PF00199	ECOD (1.6)
B	PF06628	e4e37B2	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: PF06628	ECOD (1.6)
C	PF00199	e4e37C2	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: PF00199	ECOD (1.6)
C	PF00199	e4e37C1	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: PF00199	ECOD (1.6)
C	PF06628	e4e37C3	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: PF06628	ECOD (1.6)
D	PF00199	e4e37D2	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: PF00199	ECOD (1.6)
D	PF00199	e4e37D1	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: PF00199	ECOD (1.6)
D	PF06628	e4e37D3	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: PF06628	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	IPR024708	Catalase active site	Active Site
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
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	IPR040333	Catalase, clade 3	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	OMT	Parent Component: MET RESID: AA0251 PSI-MOD : L-methionine sulfone MOD:00256

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.