2CGL

Crystal Structure of L-rhamnulose kinase from Escherichia coli in complex with L-fructose, ADP and a modeled ATP gamma phosphate.

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)
A	FGGY_C	e2cglA2	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	e2cglA1	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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	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	RHAMNULOKINASE	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 kinase activity glycerol kinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups rhamnulokinase activity carbohydrate kinase activity	carbohydrate metabolic process polyol metabolic process alditol metabolic process organic hydroxy compound metabolic process primary metabolic process metabolic process alcohol metabolic process small molecule metabolic process glycerol metabolic process rhamnose catabolic process monosaccharide metabolic process catabolic process hexose catabolic process carbohydrate catabolic process carbohydrate metabolic process polyol metabolic process alditol metabolic process organic hydroxy compound metabolic process primary metabolic process metabolic process alcohol metabolic process small molecule metabolic process glycerol metabolic process rhamnose catabolic process monosaccharide metabolic process catabolic process hexose catabolic process carbohydrate catabolic process hexose metabolic process monosaccharide catabolic process small molecule catabolic process rhamnose metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR018485	Carbohydrate kinase FGGY, C-terminal	Domain
A	IPR013449	Rhamnulokinase	Family
A	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
A	IPR018484	Carbohydrate kinase FGGY, N-terminal	Domain

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.