6NMN

Ternary complex structure of the T130K mutant of ANT-4'' with Neomycin and ATP (No Pyrophosphate)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
AMR Gene: CARD Annotation
AMR Gene Family: CARD Annotation
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6nmna2	All alpha proteins	Four-helical up-and-down bundle	Nucleotidyltransferase substrate binding subunit/domain	Kanamycin nucleotidyltransferase (KNTase), C-terminal domain	automated matches	Bacillus stearothermophilus (Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
A	d6nmna1	Alpha and beta proteins (a+b)	Nucleotidyltransferase	Nucleotidyltransferase	Kanamycin nucleotidyltransferase (KNTase), N-terminal domain	automated matches	Bacillus stearothermophilus (Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
B	d6nmnb2	All alpha proteins	Four-helical up-and-down bundle	Nucleotidyltransferase substrate binding subunit/domain	Kanamycin nucleotidyltransferase (KNTase), C-terminal domain	automated matches	Bacillus stearothermophilus (Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
B	d6nmnb1	Alpha and beta proteins (a+b)	Nucleotidyltransferase	Nucleotidyltransferase	Kanamycin nucleotidyltransferase (KNTase), N-terminal domain	automated matches	Bacillus stearothermophilus (Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	KNTase_C	e6nmnA1	A: alpha bundles	X: Four-helical up-and-down bundle	H: HEPN	T: Nucleotidyltransferase substrate binding subunit/domain	F: KNTase_C	ECOD (1.6)
A	NTP_transf_2	e6nmnA2	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: NTP_transf_2	ECOD (1.6)
B	KNTase_C	e6nmnB1	A: alpha bundles	X: Four-helical up-and-down bundle	H: HEPN	T: Nucleotidyltransferase substrate binding subunit/domain	F: KNTase_C	ECOD (1.6)
B	NTP_transf_2	e6nmnB2	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: NTP_transf_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.460.10	Alpha Beta	2-Layer Sandwich	Beta Polymerase	domain 2	CATH (utative)
A	1.20.120.330	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Nucleotidyltransferases domain 2	CATH (utative)
B	3.30.460.10	Alpha Beta	2-Layer Sandwich	Beta Polymerase	domain 2	CATH (utative)
B	1.20.120.330	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Nucleotidyltransferases domain 2	CATH (utative)

AMR Gene: CARD Annotation CARD Database Homepage

Chains	Accession	Short Name	Description	Provenance Source (Version)
A, B	ARO:3002623	ANT(4')-Ia	ANT(4')-Ia is a plasmid-encoded aminoglycoside nucleotidyltransferase in S. epidermidis, S. aureus, Enterococcus spp. and Bacillus spp.	CARD (3.3.0)

AMR Gene Family: CARD Annotation CARD Database Homepage

Chains	Accession	Gene Family	Drug Class	Resistance Machanism	Provenance Source (Version)
A, B	ARO:3000229	ANT(4')	aminoglycoside antibiotic	antibiotic inactivation	CARD (3.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF07827	KNTase C-terminal domain (KNTase_C)	KNTase C-terminal domain	Kanamycin nucleotidyltransferase (KNTase) is involved in conferring resistance to aminoglycoside antibiotics and catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit be ...	Kanamycin nucleotidyltransferase (KNTase) is involved in conferring resistance to aminoglycoside antibiotics and catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit being composed of two domains. The C-terminal domain contains five alpha helices, four of which are organised into an up-and-down alpha helical bundle. Residues found in this domain may contribute to this enzyme's active site [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Kanamycin nucleotidyltransferase	transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding ion binding binding metal ion binding small molecule binding	response to stimulus response to chemical response to antibiotic	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR043519	Nucleotidyltransferase superfamily	Homologous Superfamily
A, B	IPR012481	Kanamycin nucleotidyltransferase, C-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.