2YHW

High-resolution crystal structures of N-Acetylmannosamine kinase: Insights about substrate specificity, activity and inhibitor modelling.

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
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ROK_N	e2yhwA3	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: ROK_N	ECOD (1.6)
A	ROK_C	e2yhwA4	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: ROK_C	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	PF00480	ROK family (ROK)	ROK family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE/N-ACETYLMANNOSAMINE 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 isomerase activity racemase and epimerase activity UDP-N-acetylglucosamine 2-epimerase activity racemase and epimerase activity, acting on carbohydrates and derivatives catalytic activity hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity N-acylmannosamine kinase activity carbohydrate kinase activity kinase activity transferase activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups cation binding metal ion binding	amino sugar biosynthetic process carbohydrate derivative biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process carbohydrate derivative metabolic process amide biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process biosynthetic process N-acetylneuraminate biosynthetic process amino sugar metabolic process amino sugar biosynthetic process carbohydrate derivative biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process carbohydrate derivative metabolic process amide biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process biosynthetic process N-acetylneuraminate biosynthetic process amino sugar metabolic process small molecule metabolic process metabolic process cellular process amide metabolic process N-acetylneuraminate metabolic process nucleoside phosphate metabolic process nucleotide-sugar metabolic process primary metabolic process nucleobase-containing compound metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process UDP-N-acetylglucosamine metabolic process phosphorus metabolic process glucosamine-containing compound biosynthetic process N-acetylglucosamine metabolic process N-acetylglucosamine biosynthetic process glucosamine-containing compound metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
A	IPR003331	UDP-N-acetylglucosamine 2-epimerase domain	Domain
A	IPR020004	Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase	Family
A	IPR000600	ROK family	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q9Y223	sialuria inclusion body myositis GNE myopathy myopathy myositis ovarian cancer pancreatic intraductal papillary-mucinous neoplasm arthrogryposis subependymal giant cell astrocytoma distal myopathy inborn errors of metabolism Inclusion Body Myopathy, Sporadic limb-girdle muscular dystrophy medulloblastoma muscular disease sialuria inclusion body myositis GNE myopathy myopathy myositis ovarian cancer pancreatic intraductal papillary-mucinous neoplasm arthrogryposis subependymal giant cell astrocytoma distal myopathy inborn errors of metabolism Inclusion Body Myopathy, Sporadic limb-girdle muscular dystrophy medulloblastoma muscular disease nasopharyngeal carcinoma pancreatic ductal adenocarcinoma psoriasis congenital disorder of glycosylation lysosomal storage disease pancreatic intraductal papillary-mucinous carcinoma Salla disease spina bifida malignant colon neoplasm muscle tissue disease

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	SNN	Parent Component: ASN RESID: AA0302 , AA0593 PSI-MOD : L-aspartimide MOD:00307 , 2-(2-aminosuccinimidyl)pentanedioic acid (Asn) MOD:01940 , 2-(2-aminosuccinimidyl)pentanedioic acid (Asp) MOD:01941

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.