4BC4

Crystal structure of human D-xylulokinase in complex with D-xylulose

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	FGGY_C	e4bc4A2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: FGGY_C	ECOD (1.6)
A	FGGY_N	e4bc4A1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: FGGY_N	ECOD (1.6)
C	FGGY_C	e4bc4C2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: FGGY_C	ECOD (1.6)
C	FGGY_N	e4bc4C1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: FGGY_N	ECOD (1.6)
B	FGGY_C	e4bc4B2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: FGGY_C	ECOD (1.6)
B	FGGY_N	e4bc4B1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: FGGY_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.420.40	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
C	3.30.420.40	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
B	3.30.420.40	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00370	FGGY family of carbohydrate kinases, N-terminal domain (FGGY_N)	FGGY family of carbohydrate kinases, N-terminal domain	This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.	Domain
A, B, C	PF02782	FGGY family of carbohydrate kinases, C-terminal domain (FGGY_C)	FGGY family of carbohydrate kinases, C-terminal domain	This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	XYLULOSE KINASE	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding carbohydrate kinase activity kinase activity D-xylulokinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups	monosaccharide metabolic process carbohydrate metabolic process small molecule metabolic process metabolic process cellular process primary metabolic process xylulose metabolic process pentose metabolic process catabolic process carbohydrate catabolic process xylulose catabolic process monosaccharide catabolic process small molecule catabolic process pentose catabolic process monosaccharide metabolic process carbohydrate metabolic process small molecule metabolic process metabolic process cellular process primary metabolic process xylulose metabolic process pentose metabolic process catabolic process carbohydrate catabolic process xylulose catabolic process monosaccharide catabolic process small molecule catabolic process pentose catabolic process D-glucuronate catabolic process to D-xylulose 5-phosphate oxoacid metabolic process carbohydrate derivative metabolic process organic acid metabolic process organic acid catabolic process cellular catabolic process monocarboxylic acid catabolic process D-glucuronate catabolic process carboxylic acid catabolic process phosphate-containing compound metabolic process phosphorus metabolic process D-glucuronate metabolic process carbohydrate derivative biosynthetic process uronic acid metabolic process carboxylic acid metabolic process xylulose 5-phosphate metabolic process biosynthetic process organophosphate metabolic process glucuronate metabolic process organophosphate biosynthetic process monocarboxylic acid metabolic process xylulose 5-phosphate biosynthetic process glucuronate catabolic process generation of precursor metabolites and energy D-xylose metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
A, B, C	IPR042024	D-xylulose kinase	Family
A, B, C	IPR018485	Carbohydrate kinase FGGY, C-terminal	Domain
A, B, C	IPR000577	Carbohydrate kinase, FGGY	Family
A, B, C	IPR018484	Carbohydrate kinase FGGY, N-terminal	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C	Pharos: O75191	drug-induced liver injury pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia lung cancer psoriasis osteosarcoma

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.