3SK1

Crystal structure of phenazine resistance protein EhpR from Enterobacter agglomerans (Erwinia herbicola, Pantoea agglomerans) Eh1087, apo form

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
A	F_UNCLASSIFIED	e3sk1A1	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: F_UNCLASSIFIED	ECOD (1.6)
B	F_UNCLASSIFIED	e3sk1B1	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: F_UNCLASSIFIED	ECOD (1.6)
C	F_UNCLASSIFIED	e3sk1C1	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: F_UNCLASSIFIED	ECOD (1.6)
D	F_UNCLASSIFIED	e3sk1D1	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: F_UNCLASSIFIED	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.720.120	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1		CATH (4.3.0)
A	3.30.720.110	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1		CATH (4.3.0)
B	3.30.720.120	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1		CATH (4.3.0)
B	3.30.720.110	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1		CATH (4.3.0)
C	3.30.720.120	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1		CATH (4.3.0)
C	3.30.720.110	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1		CATH (4.3.0)
D	3.30.720.120	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1		CATH (4.3.0)
D	3.30.720.110	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00903	Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily (Glyoxalase)	Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	EhpR	organic acid binding binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity	response to stimulus response to chemical response to antibiotic	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR026275	Glyoxalase/dioxygenase/EhpR	Family
A, B, C, D	IPR029068	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Homologous Superfamily
A, B, C, D	IPR037523	Vicinal oxygen chelate (VOC) domain	Domain
A, B, C, D	IPR004360	Glyoxalase/fosfomycin resistance/dioxygenase domain	Domain

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.