1EEJ

CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE, DSBC, FROM ESCHERICHIA COLI

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1eeja1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	DsbC/DsbG C-terminal domain-like	Disulfide bond isomerase, DsbC, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1eeja2	Alpha and beta proteins (a+b)	Cystatin-like	DsbC/DsbG N-terminal domain-like	DsbC/DsbG N-terminal domain-like	Disulfide bond isomerase, DsbC, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1eejb1	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	DsbC/DsbG C-terminal domain-like	Disulfide bond isomerase, DsbC, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1eejb2	Alpha and beta proteins (a+b)	Cystatin-like	DsbC/DsbG N-terminal domain-like	DsbC/DsbG N-terminal domain-like	Disulfide bond isomerase, DsbC, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	DsbC/DsbG C-terminal domain-like	8032013	4000486	SCOP2 (2022-06-29)
A	SCOP2 Family	DsbC/DsbG N-terminal domain-like	8022285	4001018	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thioredoxin-like	8044391	3000031	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	DsbC/DsbG N-terminal domain-like	8034665	3000466	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	DsbC/DsbG N-terminal domain-like	8034665	3000466	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin-like	8044391	3000031	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	DsbC_N	e1eejA1	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: DsbC_N	ECOD (1.6)
A	DSBA_1	e1eejA2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: DSBA_1	ECOD (1.6)
B	DsbC_N	e1eejB1	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: DsbC_N	ECOD (1.6)
B	DSBA_1	e1eejB2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: DSBA_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.450.70	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
B	3.10.450.70	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
B	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	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	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	THIOL:DISULFIDE INTERCHANGE PROTEIN	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity oxidoreductase activity catalytic activity, acting on a protein protein-disulfide reductase activity catalytic activity isomerase activity intramolecular oxidoreductase activity intramolecular oxidoreductase activity, transposing S-S bonds identical protein binding protein binding binding protein homodimerization activity protein dimerization activity oxidoreductase activity, acting on a sulfur group of donors disulfide oxidoreductase activity oxidoreductase activity catalytic activity, acting on a protein protein-disulfide reductase activity catalytic activity isomerase activity intramolecular oxidoreductase activity intramolecular oxidoreductase activity, transposing S-S bonds protein disulfide isomerase activity	response to copper ion response to stimulus response to metal ion response to chemical response to inorganic substance organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression chaperone-mediated protein folding macromolecule biosynthetic process protein maturation organic substance metabolic process response to copper ion response to stimulus response to metal ion response to chemical response to inorganic substance organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression chaperone-mediated protein folding macromolecule biosynthetic process protein maturation organic substance metabolic process protein folding biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process	periplasmic space cellular anatomical entity outer membrane-bounded periplasmic space cell envelope

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013766	Thioredoxin domain	Domain
A, B	IPR012336	Thioredoxin-like fold	Domain
A, B	IPR017937	Thioredoxin, conserved site	Conserved Site
A, B	IPR033954	Disulphide bond isomerase, DsbC/G	Family
A, B	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A, B	IPR018950	Disulphide bond isomerase, DsbC/G, N-terminal	Domain
A, B	IPR009094	Disulphide bond isomerase DsbC/G, N-terminal domain superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	protein disulfide-isomerase (DsbC) M-CSA #512	The disulphide bond isomerase DsbC from E. coli is able to break up incorrectly formed disulphide bonds by transferring electrons to reduce the bond. It displays homology to the thioredoxase family of enzymes.	Defined by 4 residues: ASP:A-95CYS:A-98CYS:A-101ARG:A-125 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.3.4.1 (PDB Primary Data) Search M-CSA Motif + EC 5.3.4.1

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.