4ML6

Disulfide isomerase from multidrug resistance IncA/C conjugative plasmid in reduced state

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	PF10411	e4ml6A2	A: a+b two layers	X: Cystatin-like	H: DsbC/DsbG N-terminal domain-like (From Topology)	T: DsbC/DsbG N-terminal domain-like	F: PF10411	ECOD (1.6)
A	PF13098	e4ml6A1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF13098	ECOD (1.6)
B	PF10411	e4ml6B2	A: a+b two layers	X: Cystatin-like	H: DsbC/DsbG N-terminal domain-like (From Topology)	T: DsbC/DsbG N-terminal domain-like	F: PF10411	ECOD (1.6)
B	PF13098	e4ml6B1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF13098	ECOD (1.6)
C	PF10411	e4ml6C2	A: a+b two layers	X: Cystatin-like	H: DsbC/DsbG N-terminal domain-like (From Topology)	T: DsbC/DsbG N-terminal domain-like	F: PF10411	ECOD (1.6)
C	PF13098	e4ml6C1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF13098	ECOD (1.6)
D	PF10411	e4ml6D2	A: a+b two layers	X: Cystatin-like	H: DsbC/DsbG N-terminal domain-like (From Topology)	T: DsbC/DsbG N-terminal domain-like	F: PF10411	ECOD (1.6)
D	PF13098	e4ml6D1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PF13098	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
B	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
C	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
D	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF10411	Disulfide bond isomerase protein N-terminus (DsbC_N)	Disulfide bond isomerase protein N-terminus	This is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of t ...	This is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of the V, so are vital for dimerisation [1]. DsbC is required for disulfide bond formation and functions as a disulfide bond isomerase during oxidative protein-folding in bacterial periplasm. It also has chaperone activity [2].	Domain
A, B, C, D	PF13098	Thioredoxin-like domain (Thioredoxin_2)	Thioredoxin-like domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	DsbP	isomerase activity catalytic activity	-	periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR012336	Thioredoxin-like fold	Domain
A, B, C, D	IPR033954	Disulphide bond isomerase, DsbC/G	Family
A, B, C, D	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A, B, C, D	IPR018950	Disulphide bond isomerase, DsbC/G, N-terminal	Domain
A, B, C, D	IPR009094	Disulphide bond isomerase DsbC/G, N-terminal domain superfamily	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 R01GM133198.