3O3W

Crystal Structure of BH2092 protein (residues 14-131) from Bacillus halodurans, Northeast Structural Genomics Consortium Target BhR228A

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family 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	PF00581	e3o3wA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)
B	PF00581	e3o3wB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)
C	PF00581	e3o3wC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)
D	PF00581	e3o3wD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)
E	PF00581	e3o3wE1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)
F	PF00581	e3o3wF1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)
G	PF00581	e3o3wG1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)
H	PF00581	e3o3wH1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)
I	PF00581	e3o3wI1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Rhodanese/Cell cycle control phosphatase	F: PF00581	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)
B	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)
C	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)
D	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)
E	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)
F	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)
G	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)
H	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)
I	3.40.250.10	Alpha Beta	3-Layer(aba) Sandwich	Oxidized Rhodanese	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I	PF00581	Rhodanese-like domain (Rhodanese)	Rhodanese-like domain	Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.	Domain

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR001763	Rhodanese-like domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR036873	Rhodanese-like domain superfamily	Homologous Superfamily

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.