4ORK | pdb_00004ork

Crystal Structure of the Phosphotransferase Domain of the Bifunctional Aminoglycoside Resistance Enzyme AAC(6')-Ie-APH(2'')-Ia

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
D	Fructosamin_kin	e4orkD1	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)
C	Fructosamin_kin	e4orkC1	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)
B	Fructosamin_kin	e4orkB1	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)
A	Fructosamin_kin	e4orkA1	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)
D	3.30.200.20	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
D	3.90.1200.10	Alpha Beta	Alpha-Beta Complex	Aminoglycoside 3'-phosphotransferase	Chain: A, domain 2	CATH (4.3.0)
C	3.30.200.20	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
C	3.90.1200.10	Alpha Beta	Alpha-Beta Complex	Aminoglycoside 3'-phosphotransferase	Chain: A, domain 2	CATH (4.3.0)
B	3.30.200.20	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
B	3.90.1200.10	Alpha Beta	Alpha-Beta Complex	Aminoglycoside 3'-phosphotransferase	Chain: A, domain 2	CATH (4.3.0)
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)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Bifunctional AAC/APH	kinase activity aminoglycoside phosphotransferase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups N-acyltransferase activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding kinase activity aminoglycoside phosphotransferase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups N-acyltransferase activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding	response to stimulus response to chemical response to antibiotic	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A, B, C, D	IPR000182	GNAT domain	Domain
A, B, C, D	IPR002575	Aminoglycoside phosphotransferase	Domain
A, B, C, D	IPR011009	Protein kinase-like domain superfamily	Homologous Superfamily

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.