6B0U

Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with a Lys-containing peptide

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)
B	PF13530	e6b0uB3	A: a+b two layers	X: Sterol carrier protein-like	H: Sterol carrier protein, SCP-related (From Topology)	T: Sterol carrier protein, SCP-related	F: PF13530	ECOD (1.6)
B	PF13527	e6b0uB2	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: PF13527	ECOD (1.6)
B	PF17668	e6b0uB1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: PF17668	ECOD (1.6)
A	PF13530	e6b0uA1	A: a+b two layers	X: Sterol carrier protein-like	H: Sterol carrier protein, SCP-related (From Topology)	T: Sterol carrier protein, SCP-related	F: PF13530	ECOD (1.6)
A	PF13527	e6b0uA2	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: PF13527	ECOD (1.6)
A	PF17668	e6b0uA3	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: PF17668	ECOD (1.6)
C	PF13530	e6b0uC2	A: a+b two layers	X: Sterol carrier protein-like	H: Sterol carrier protein, SCP-related (From Topology)	T: Sterol carrier protein, SCP-related	F: PF13530	ECOD (1.6)
C	PF13527	e6b0uC1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: PF13527	ECOD (1.6)
C	PF17668	e6b0uC3	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: PF17668	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
B	3.30.1050.10	Alpha Beta	2-Layer Sandwich	Nonspecific Lipid-transfer Protein	Chain A	CATH (4.3.0)
A	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
A	3.30.1050.10	Alpha Beta	2-Layer Sandwich	Nonspecific Lipid-transfer Protein	Chain A	CATH (4.3.0)
C	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
C	3.30.1050.10	Alpha Beta	2-Layer Sandwich	Nonspecific Lipid-transfer Protein	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF13527	Acetyltransferase (GNAT) domain (Acetyltransf_9)	Acetyltransferase (GNAT) domain	This domain catalyses N-acetyltransferase reactions.	Domain
A, B, C	PF13530	Sterol carrier protein domain (SCP2_2)	Sterol carrier protein domain	-	Domain
A, B, C	PF17668	Acetyltransferase (GNAT) domain (Acetyltransf_17)	Acetyltransferase (GNAT) domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	N-acetyltransferase Eis	acetyltransferase activity N-acetyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity N-acyltransferase activity peptide-lysine-N-acetyltransferase activity catalytic activity, acting on a protein peptide N-acetyltransferase activity aminoglycoside N-acetyltransferase activity identical protein binding protein binding binding	symbiont-mediated perturbation of host defense response symbiont-mediated perturbation of host defense-related programmed cell death response to host defenses symbiont-mediated perturbation of host cellular process biological process involved in interspecies interaction between organisms response to stimulus symbiont-mediated suppression of host defense-related programmed cell death response to other organism symbiont-mediated perturbation of host programmed cell death response to defenses of other organism symbiont-mediated perturbation of host defenses symbiont-mediated suppression of host programmed cell death response to external stimulus response to biotic stimulus biological process involved in interaction with host symbiont-mediated perturbation of host defense response symbiont-mediated perturbation of host defense-related programmed cell death response to host defenses symbiont-mediated perturbation of host cellular process biological process involved in interspecies interaction between organisms response to stimulus symbiont-mediated suppression of host defense-related programmed cell death response to other organism symbiont-mediated perturbation of host programmed cell death response to defenses of other organism symbiont-mediated perturbation of host defenses symbiont-mediated suppression of host programmed cell death response to external stimulus response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction modulation by symbiont of host process symbiont-mediated suppression of host defenses cellular process response to host response to external biotic stimulus modulation of process of another organism carbohydrate derivative catabolic process glycosyl compound metabolic process catabolic process aminoglycoside antibiotic catabolic process glycoside metabolic process carbohydrate derivative metabolic process glycosyl compound catabolic process antibiotic catabolic process glycoside catabolic process antibiotic metabolic process organic substance metabolic process aminoglycoside antibiotic metabolic process metabolic process organic substance catabolic process response to chemical response to antibiotic symbiont-mediated perturbation of host inflammatory response cellular response to stimulus cellular response to oxidative stress cellular response to chemical stress cellular response to stress response to stress response to host immune response symbiont defense to host-produced reactive oxygen species symbiont-mediated perturbation of host innate immune response symbiont-mediated perturbation of host immune response effector-mediated defense to host-produced reactive oxygen species response to oxidative stress cellular response to chemical stimulus	membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle cellular anatomical entity bacterial extracellular vesicle vesicle extracellular membrane-bounded organelle host extracellular space host cellular component intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle cellular anatomical entity bacterial extracellular vesicle vesicle extracellular membrane-bounded organelle host extracellular space host cellular component intracellular anatomical structure cytoplasm cytosol host cell cytoplasmic vesicle host intracellular membrane-bounded organelle host intracellular part host cell cytoplasm host cell part host intracellular region host cell cytoplasm part host intracellular organelle
D, E	Synthetic peptide ATKAPAKKA	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR025559	Enhanced intracellular survival protein domain	Domain
A, B, C	IPR000182	GNAT domain	Domain
A, B, C	IPR022902	N-acetyltransferase Eis	Family
A, B, C	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A, B, C	IPR036527	SCP2 sterol-binding domain superfamily	Homologous Superfamily
A, B, C	IPR041380	Eis-like, acetyltransferase domain	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 R01GM133198.