5FTG

Human choline kinase a1 in complex with compound 1-[[4-[2-[4-[[4-(dimethylamino)pyridin-1- yl]methyl]phenoxy]ethoxy]phenyl]methyl]-N,N- dimethyl-pyridin-4-amine (compound 10a)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5ftga_	Alpha and beta proteins (a+b)	Protein kinase-like (PK-like)	Protein kinase-like (PK-like)	Choline kinase	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Protein kinase-like (PK-like)	8085227	3000066	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Fructosamin_kin	e5ftgA1	A: a+b complex topology	X: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)	H: Protein kinase/SAICAR synthase/ATP-grasp	T: Protein kinase	F: Fructosamin_kin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.200.20	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
A	3.90.1200.10	Alpha Beta	Alpha-Beta Complex	Aminoglycoside 3'-phosphotransferase	Chain: A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01633	Choline/ethanolamine kinase (Choline_kinase)	Choline/ethanolamine kinase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CHOLINE KINASE ALPHA	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 hydrolase activity, acting on ester bonds cholinesterase activity carboxylic ester hydrolase activity hydrolase activity catalytic activity identical protein binding protein binding protein homodimerization activity protein dimerization activity ethanolamine kinase activity kinase activity transferase activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups choline kinase activity protein tyrosine kinase activity catalytic activity, acting on a protein protein kinase activity	glycerophospholipid biosynthetic process cellular biosynthetic process cellular metabolic process glycerophospholipid metabolic process lipid biosynthetic process primary metabolic process phospholipid biosynthetic process phospholipid metabolic process biosynthetic process glycerolipid biosynthetic process organophosphate metabolic process organophosphate biosynthetic process cellular lipid metabolic process phosphate-containing compound metabolic process phosphatidylcholine metabolic process glycerophospholipid biosynthetic process cellular biosynthetic process cellular metabolic process glycerophospholipid metabolic process lipid biosynthetic process primary metabolic process phospholipid biosynthetic process phospholipid metabolic process biosynthetic process glycerolipid biosynthetic process organophosphate metabolic process organophosphate biosynthetic process cellular lipid metabolic process phosphate-containing compound metabolic process phosphatidylcholine metabolic process glycerolipid metabolic process metabolic process cellular process phosphatidylcholine biosynthetic process phosphorus metabolic process lipid metabolic process cellular response to stimulus cellular response to nutrient levels response to nutrient levels response to stimulus cellular response to stress response to stress response to starvation cellular response to glucose starvation cellular response to starvation cellular component organization cellular component disassembly organelle organization organelle disassembly lipid droplet disassembly lipid droplet organization cellular component organization or biogenesis localization transport macromolecule localization lipid localization lipid transport establishment of localization CDP-choline pathway phosphatidylethanolamine metabolic process phosphatidylethanolamine biosynthetic process	lipid droplet intracellular organelle intracellular anatomical structure organelle intracellular non-membrane-bounded organelle cellular anatomical entity non-membrane-bounded organelle cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011009	Protein kinase-like domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P35790	spina bifida esophageal adenocarcinoma malignant mesothelioma Pick disease Status Dysraphicus lung cancer osteosarcoma tethered spinal cord syndrome malignant ependymoma pancreatic ductal adenocarcinoma ulcerative colitis

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.