7DLK

Crystal Structure of veratryl alcohol bound Dye Decolorizing peroxidase from Bacillus subtilis

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Dyp_perox_C	e7dlkB1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_C	ECOD (1.6)
B	Dyp_perox_N_1	e7dlkB2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_N_1	ECOD (1.6)
C	Dyp_perox_C	e7dlkC1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_C	ECOD (1.6)
C	Dyp_perox_N_1	e7dlkC2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_N_1	ECOD (1.6)
E	Dyp_perox_C	e7dlkE1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_C	ECOD (1.6)
E	Dyp_perox_N_1	e7dlkE2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_N_1	ECOD (1.6)
A	Dyp_perox_C	e7dlkA1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_C	ECOD (1.6)
A	Dyp_perox_N_1	e7dlkA2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_N_1	ECOD (1.6)
D	Dyp_perox_C	e7dlkD1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_C	ECOD (1.6)
D	Dyp_perox_N_1	e7dlkD2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_N_1	ECOD (1.6)
F	Dyp_perox_C	e7dlkF1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_C	ECOD (1.6)
F	Dyp_perox_N_1	e7dlkF2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: Dyp_perox_N_1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF04261	Dyp-type peroxidase, N-terminal (Dyp_perox_N)	Dyp-type peroxidase, N-terminal	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much ...	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much lower pH conditions compared with the other plant peroxidases [2,3,4]. They consist of two domains that adopt a ferredoxin-like fold [2,4], connected by a loop. This entry represents the N-terminal domain [2,3,4].	Domain
A, B, C, D, E A, B, C, D, E, F	PF20628	Dyp-type peroxidase, C-terminal (Dyp_perox_C)	Dyp-type peroxidase, C-terminal	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much ...	Dyp-type (dye-decolorizing) peroxidases are a family of heme proteins found in a wide range of bacteria and fungi [1,2]. They have a wide substrate specificity and lack homology to most other peroxidases, with the ability to function well under much lower pH conditions compared with the other plant peroxidases [2,3,4]. They consist of two domains that adopt a ferredoxin-like fold [2,4], connected by a loop. This entry represents the C-terminal domain, which possess a large hydrophobic cavity for heme binding [2,3,4].	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	Deferrochelatase/peroxidase	lyase activity ferrochelatase activity catalytic activity peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding lyase activity ferrochelatase activity catalytic activity peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding ion binding metal ion binding small molecule binding	cellular localization inorganic ion homeostasis iron import into cell homeostatic process transport iron ion transport establishment of localization metal ion transport localization intracellular iron ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis establishment of localization in cell monoatomic ion homeostasis cellular localization inorganic ion homeostasis iron import into cell homeostatic process transport iron ion transport establishment of localization metal ion transport localization intracellular iron ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis establishment of localization in cell monoatomic ion homeostasis intracellular chemical homeostasis transition metal ion transport monoatomic ion transport cellular process monoatomic cation homeostasis monoatomic cation transport intracellular monoatomic ion homeostasis	cellular anatomical structure extracellular region intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR048327	Dyp-type peroxidase, N-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR006313	Deferrochelatase	Family
A, B, C, D, E A, B, C, D, E, F	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR048328	Dyp-type peroxidase, C-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR006314	Dyp-type peroxidase	Family
A, B, C, D, E A, B, C, D, E, F	IPR019546	Twin-arginine translocation pathway, signal sequence, bacterial/archaeal	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR011008	Dimeric alpha-beta barrel	Homologous Superfamily

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.