3IHG

Crystal structure of a ternary complex of aklavinone-11 hydroxylase with FAD and aklavinone

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)
B	FAD_binding_3_2nd	e3ihgB2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: FAD_binding_3_2nd	ECOD (1.6)
B	PRK06126_2nd	e3ihgB3	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PRK06126_2nd	ECOD (1.6)
B	FAD_binding_3_1st	e3ihgB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
C	FAD_binding_3_2nd	e3ihgC3	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: FAD_binding_3_2nd	ECOD (1.6)
C	PRK06126_2nd	e3ihgC2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PRK06126_2nd	ECOD (1.6)
C	FAD_binding_3_1st	e3ihgC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)
A	FAD_binding_3_2nd	e3ihgA3	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: FAD_binding_3_2nd	ECOD (1.6)
A	PRK06126_2nd	e3ihgA2	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: PRK06126_2nd	ECOD (1.6)
A	FAD_binding_3_1st	e3ihgA4	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: FAD_binding_3_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
B	3.30.9.10	Alpha Beta	2-Layer Sandwich	D-Amino Acid Oxidase	Chain A, domain 2	CATH (4.3.0)
B	3.40.30.120	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin		CATH (4.3.0)
C	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
C	3.30.9.10	Alpha Beta	2-Layer Sandwich	D-Amino Acid Oxidase	Chain A, domain 2	CATH (4.3.0)
C	3.40.30.120	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin		CATH (4.3.0)
A	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
A	3.30.9.10	Alpha Beta	2-Layer Sandwich	D-Amino Acid Oxidase	Chain A, domain 2	CATH (4.3.0)
A	3.40.30.120	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF21274	Aromatic-ring hydroxylase, C-terminal (Rng_hyd_C)	Aromatic-ring hydroxylase, C-terminal	This is a thioredoxin-like domain found at the C-terminal of aromatic-ring hydroxylases [1-5], such as PgaE from Bacillus subtilis and Rifampicin monooxygenase from Streptomyces venezuelae. The function of this domain is not clear. It may be involved ...	This is a thioredoxin-like domain found at the C-terminal of aromatic-ring hydroxylases [1-5], such as PgaE from Bacillus subtilis and Rifampicin monooxygenase from Streptomyces venezuelae. The function of this domain is not clear. It may be involved in folding and stability [6] as it lacks the catalytic cysteine residues of thioredoxin, therefore, is not likely to have a redox function [1].	Domain
A, B, C	PF01494	FAD binding domain (FAD_binding_3)	FAD binding domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	RdmE	FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen catalytic activity	aminoglycoside antibiotic biosynthetic process glycosyl compound metabolic process ketone metabolic process polyketide metabolic process carbohydrate derivative metabolic process antibiotic biosynthetic process secondary metabolic process antibiotic metabolic process secondary metabolite biosynthetic process small molecule metabolic process carbohydrate derivative biosynthetic process glycosyl compound biosynthetic process daunorubicin metabolic process small molecule biosynthetic process aminoglycoside antibiotic biosynthetic process glycosyl compound metabolic process ketone metabolic process polyketide metabolic process carbohydrate derivative metabolic process antibiotic biosynthetic process secondary metabolic process antibiotic metabolic process secondary metabolite biosynthetic process small molecule metabolic process carbohydrate derivative biosynthetic process glycosyl compound biosynthetic process daunorubicin metabolic process small molecule biosynthetic process glycoside metabolic process glycoside biosynthetic process daunorubicin biosynthetic process biosynthetic process aminoglycoside antibiotic metabolic process polyketide biosynthetic process metabolic process cellular process ketone biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR002938	FAD-binding domain	Domain
A, B, C	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C	IPR050641	Rifampicin monooxygenase-like	Family

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 R01GM157729.