4IX1

Crystal structure of hypothetical protein OPAG_01669 from Rhodococcus Opacus PD630, Target 016205

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	COG3473_1	e4ix1A2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: COG3473_1	ECOD (1.6)
A	AroM	e4ix1A3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: AroM	ECOD (1.6)
B	COG3473_1	e4ix1B2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: COG3473_1	ECOD (1.6)
B	AroM	e4ix1B3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: AroM	ECOD (1.6)
D	COG3473_1	e4ix1D1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: COG3473_1	ECOD (1.6)
D	AroM	e4ix1D7	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: AroM	ECOD (1.6)
E	COG3473_1	e4ix1E2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: COG3473_1	ECOD (1.6)
E	AroM	e4ix1E5	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: AroM	ECOD (1.6)
F	COG3473_1	e4ix1F1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: COG3473_1	ECOD (1.6)
F	AroM	e4ix1F2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: AroM	ECOD (1.6)
G	COG3473_1	e4ix1G1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: COG3473_1	ECOD (1.6)
G	AroM	e4ix1G7	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: AroM	ECOD (1.6)
H	COG3473_1	e4ix1H2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: COG3473_1	ECOD (1.6)
H	AroM	e4ix1H7	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: AroM	ECOD (1.6)
C	COG3473_1	e4ix1C1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: COG3473_1	ECOD (1.6)
C	AroM	e4ix1C7	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: ATC-like	F: AroM	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.12500	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.12500	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	3.40.50.12500	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
E	3.40.50.12500	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
F	3.40.50.12500	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
G	3.40.50.12500	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
H	3.40.50.12500	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	3.40.50.12500	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		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	PF17645	Arylmalonate decarboxylase (Amdase)	Arylmalonate decarboxylase	-	Family

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR026286	Maleate isomerase/Arylmalonate decarboxylase	Family

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.